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Review

From Waste to Wonder: Valorization of Colombian Plant By-Products for Peroxidase Production and Biotechnological Innovation

by
John J. Castillo
Escuela de Química, Universidad Industrial de Santander, Bucaramanga 680002, Colombia
Processes 2025, 13(10), 3198; https://doi.org/10.3390/pr13103198
Submission received: 10 September 2025 / Revised: 4 October 2025 / Accepted: 7 October 2025 / Published: 8 October 2025
(This article belongs to the Special Issue Enzyme Production Using Industrial and Agricultural By-Products)
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Abstract

The valorization of agricultural by-products represents a sustainable strategy to reduce waste and create high-value biotechnological products. This review highlights Colombian plant-derived peroxidases (PODs) obtained from Guinea grass, royal palm, African oil palm, lemongrass, sleepy plant, and sweet potato. These enzymes catalyze oxidative reactions and show potential in biosensing, polymer synthesis, environmental remediation, and health monitoring. We summarize extraction and purification strategies while addressing current challenges such as operational stability, scalability, and cost. Special emphasis is given to applications like cross-linked enzymatic aggregates (CLEAs) and electrochemical biosensors, where Colombian PODs demonstrate superior stability and sensitivity compared to horseradish peroxidase (HRP). This review frames these advances within the circular bioeconomy, presenting insights into waste reduction and CO2 savings. By integrating local biodiversity into innovative processes, Colombian PODs can drive sustainable technologies and provide industrial and environmental solutions.

1. Introduction

The global shift toward sustainability has intensified interest in innovative strategies to repurpose agricultural residues [1,2,3]. These by-products, including crop residues, peels, leaves, and stems, are often discarded or burned, contributing to pollution and greenhouse gas emissions [3,4,5,6,7]. However, this organic waste contains valuable biomolecules such as enzymes, proteins, and fibers that can be repurposed for high-value applications. The concept of waste valorization, particularly in the context of the circular bioeconomy, involves transforming these by-products into new products that can be reintegrated into the economy, thus extending the lifecycle of the original resource [5,8,9]. The circular bioeconomy is a model that emphasizes the sustainable management of biological resources through the reuse, recycling, and regeneration of materials [8,10]. In the context of agriculture, this means finding innovative ways to utilize by-products that are often discarded, thereby reducing the environmental footprint of agricultural activities while adding value to waste materials [2,3,11]. Agricultural by-products, which are often rich in bioactive compounds, represent a promising source of raw materials for the production of enzymes, biopolymers, and other high-value chemicals [5,12].
Colombia, recognized for its biodiversity and strong agricultural economy, generates large volumes of plant-based residues that remain underutilized. Extracting peroxidases (PODs) from these materials represents a dual opportunity: reducing waste and developing sustainable enzymes for industry [13]. In recent years, PODs have garnered significant attention for their role in various industrial and environmental processes [14]. These enzymes have been employed in biosensing technologies, where they facilitate the detection of H2O2, a critical marker in many biochemical reactions. Additionally, as is shown in Figure 1, PODs have shown promise in the synthesis of advanced materials, such as conducting polymers like polyaniline (PANI) [15], further extending their utility in material science. Their capacity to form cross-linked enzymatic aggregates (CLEAs) [16] also makes them valuable tools for bioremediation, particularly in the removal of industrial pollutants such as dyes, as well as their use in chemiluminescence assays. The biotechnological potential of PODs extracted from Colombian plant by-products represents a convergence of waste valorization and innovation. Plants such as Guinea grass (Panicum maximum), royal palm (Roystonea regia), African oil palm (Eleais guineensis), lemongrass (Cymbpogon citratus), sleepy plant (Mimosa pudica), and sweet potato (Ipomea batatas) produce significant amounts of agricultural waste [17,18,19,20]. By extracting and purifying PODs from these plants, researchers can harness their enzymatic properties for a variety of applications, contributing to both a reduction in waste and the development of sustainable technologies.
In Colombia, where agriculture plays a vital role in the national economy, the potential for waste valorization is particularly high. The country’s diverse ecosystems and wide variety of crops generate substantial amounts of plant-based by-products that could be repurposed for biotechnological applications. By leveraging the biochemical properties of enzymes like POD, Colombia can contribute to global efforts in sustainability while also fostering innovation in sectors such as environmental remediation and health monitoring [1,21].
PODs are a class of enzymes that catalyze the oxidation of various substrates in the presence of H2O2. These enzymes are widely distributed in plants and play an important role in defense mechanisms against environmental stress [22,23]. In biotechnological contexts, PODs are valued for their ability to facilitate oxidative reactions, making them useful in a range of applications including biosensors, polymer synthesis, and bioremediation [24,25].
As is shown in Figure 2, Colombian plants such as Guinea grass (Panicum maximum), Royal palm (Roystonea regia), African palm (Elaeis guineensis), lemongrass (Cymbopogon citratus), sleepy plant (Mimosa pudica), and sweet potato (Ipomoea batatas) are rich sources of PODs.
These plants produce significant agricultural by-products that can be exploited for enzyme extraction, turning waste into valuable biotechnological resources. The extraction and purification of PODs from these plants not only contribute to waste valorization but also provide a renewable source of enzymes for industrial applications [26].
Finally, the valorization of Colombian plant by-products for POD production represents a powerful example of how waste can be transformed into valuable resources within the framework of the circular bioeconomy. By harnessing the biochemical properties of peroxidases, researchers can develop innovative solutions to pressing environmental and industrial challenges. From biosensing technologies to environmental remediation, the applications of these enzymes are vast and diverse.
The purpose of this review is to provide a comprehensive overview of the current state of the research on peroxidase extraction from Colombian plant by-products, showcasing their potential as a renewable and sustainable source of enzymes for various biotechnological applications. This review highlights the potential of Colombian plant by-products as a renewable source of PODs, encouraging further research and development in this promising field. Despite the promising potential of Colombian plant-derived PODs, significant research gaps remain. First, there is a lack of comprehensive kinetic modeling to better understand the catalytic mechanisms of these enzymes, which is crucial for optimizing their performance in industrial and biosensing applications. Second, structural characterization studies, such as X-ray crystallography and molecular dynamics simulations, are limited, hindering insights into the relationship between enzyme structure and function. Finally, there is an evident scarcity of large-scale application studies aimed at transitioning these findings from laboratory settings to real-world industrial or environmental processes. Addressing these gaps is essential to fully unlocking the biotechnological potential of Colombian PODs and to fostering innovations aligned with the circular bioeconomy framework.

2. Agricultural By-Products as a Source of Peroxidases

Colombia’s rich and diverse agricultural landscape is a key pillar of the country’s economy, contributing significantly to both domestic markets and international trade. With its favorable climate and vast ecosystems, Colombia produces a variety of crops, generating large quantities of agricultural by-products [13,27,28,29,30]. These by-products, traditionally considered waste, are now recognized as valuable resources that can be valued for biotechnological and industrial applications. Waste valorization of these by-products not only contributes to sustainability but also adds value to agricultural production, supporting the circular bioeconomy. Several key plants and their by-products stand out for their potential in areas like energy, food, and biotechnology. Sakharov y cols., conducted a preliminary study to analyses the enzymatic activity of various Colombian plant species, including their leaves, fruits, and roots (Table 1) [31]. This research marked one of the earliest explorations into the potential of Colombian flora for biotechnological applications. The study focused on the extraction of enzymes such as PODs. The findings highlighted the rich enzymatic diversity present in Colombian plants and opened the door to further investigations into their potential for waste valorization and sustainable production. Building on this foundational research, the focus on agricultural by-products as a source of valuable enzymes has continued to grow, driving advancements in both scientific understanding and practical applications. The study identified several plant species that exhibited particularly promising enzymatic activity, making them strong candidates for further exploration in biotechnological applications. Among these, Guinea grass, royal palm, African palm, lemongrass, sleepy plant, and sweet potato stood out for their significant potential in enzyme production and waste valorization.

2.1. Guinea Grass (Panicum maximum)

It is widely cultivated in Colombia, particularly in the livestock sector. It serves as high-quality fodder for cattle, but the leftover biomass, such as stems and leaves, often remains underutilized [17]. Valorization of these by-products can include the production of bioenergy through anaerobic digestion, turning waste into biogas, and extraction of fibers for biodegradable packaging materials. Additionally, Guinea grass has been explored for its potential in phytoremediation, where it is used to clean contaminated soils, contributing to environmental sustainability.

2.2. Royal Palm (Roystonea regia)

This is another species that produces significant agricultural by-products, primarily from its fronds and seeds. Traditionally, these materials have been discarded or used as mulch, but recent advances have explored their use in biochar production, which can serve as a soil enhancer and carbon sequestration tool. Royal palm by-products can also be transformed into activated carbon, which is highly effective in water purification processes, adding environmental and economic value to this previously wasted material [18,32,33].

2.3. African Palm (Elaeis guineensis)

This plays a crucial role in Colombia’s economy as a major source of palm oil. However, the industry generates large amounts of by-products, including empty fruit bunches, palm kernel shells, and fibers. These residues can be valorized in various ways, such as converting them into biofuels or using them in the production of biocomposites [18]. Palm oil mill effluent, a liquid by-product, is rich in nutrients and can be treated to produce biogas or used in the production of organic fertilizers, promoting a closed-loop system in agriculture.

2.4. Lemongrass (Cymbopogon citratus)

This is known for its essential oils, which are widely used in the fragrance and food industries. The remaining biomass, such as leaves and stalks, can be repurposed through extraction of bioactive compounds, including antioxidants and antimicrobial agents. Lemongrass waste has also shown promise in bioenergy production, where it can be converted into bioethanol or used as a raw material to produce natural fibers [33,34,35,36].

2.5. Sleepy Plant (Mimosa pudica)

This species, with unique movement in response to touch, is often used for medicinal purposes in Colombia. Its leaves, stems, and roots contain compounds with antibacterial, antifungal, and anti-inflammatory properties, making it a potential source for pharmaceutical and cosmetic applications. Waste valorization efforts can focus on extracting these bioactive compounds for commercial use, reducing environmental waste while creating high-value products [37,38,39].

2.6. Sweet Potato (Ipomea batata)

This is a staple crop in Colombia, and its peels and other by-products can be repurposed in various ways. Sweet potato peels are rich in starch and antioxidants, making them valuable for food additives or as a substrate for microbial fermentation in bioethanol production. The valorization of sweet potato by-products aligns with the circular bioeconomy by reducing food waste and creating new value chains in food, energy, and material science industries [20,40,41,42,43].

3. Peroxidases: Definition, Purification and Biochemical Properties

3.1. Peroxidases

PODs are a diverse group of enzymes that catalyze the oxidation of various substrates by H2O2 as an electron acceptor. These heme-containing enzymes play critical roles in both plants and animals, though their functions in plants are particularly significant. In plants, peroxidases are primarily involved in defense mechanisms, growth regulation, and the metabolism of reactive oxygen species (ROS) [14,44]. The biological role of peroxidases is closely linked to their ability to detoxify H2O2, a by-product of various metabolic processes that can cause oxidative damage to cells. By breaking down H2O2 into water and oxygen, PODs help mitigate oxidative stress, protecting cellular components such as lipids, proteins, and DNA from damage. In addition to their role in oxidative stress management, peroxidases are also essential for lignin biosynthesis, a process critical for cell wall formation and the structural integrity of plants. Lignin strengthens plant tissues and contributes to water transport by making cell walls less permeable to water [45]. Furthermore, PODs participate in wound healing, pathogen defense, and the modulation of hormone levels, which impacts plant growth and development. In response to biotic and abiotic stresses, peroxidases facilitate the cross-linking of cell wall components, enhancing the plant’s defensive barrier against pathogens [22,46]. The enzymatic activity of PODs is defined by their ability to transfer electrons from a wide variety of donor molecules, such as phenolic compounds, to hydrogen peroxide. This reaction not only helps in the degradation of H2O2 but also contributes to the oxidative polymerization of organic molecules, including lignin precursors. The broad substrate specificity of peroxidases allows them to participate in diverse physiological processes, making them versatile enzymes with substantial importance in plant biology.

3.2. Extraction and Purification Techniques

The extraction and purification of PODs are crucial steps in studying their structure, function, and potential biotechnological applications. Due to the widespread occurrence of PODs in various plant tissues, isolating these enzymes involves selecting appropriate sources and employing techniques that maximize yield and purity while preserving enzymatic activity. The extraction process typically begins with the disruption of plant tissues to release intracellular enzymes, followed by a series of purification steps designed to separate PODs from other proteins and impurities. Common purification methods include precipitation, dialysis, chromatography, and ultrafiltration, each tailored to exploit the unique biochemical properties of PODs such as molecular weight, charge, and hydrophobicity. A well-designed extraction and purification protocol is essential for obtaining peroxidases in sufficient quantities and purity for further biochemical characterization and practical applications.
The purification of PODs from Colombian tropical plants has yielded promising results, with several species demonstrating high enzymatic activity. Among these, the leaves of the royal palm have proven to be a particularly rich source of POD, leading to the isolation of a novel enzyme with high purity. The purification process for this POD involved several key steps. Initially, the palm leaves were homogenized, and ammonium sulfate ((NH4)2SO4) precipitation was used to concentrate the enzyme while removing unwanted proteins [47]. Following this, colored compounds were extracted to reduce interference during the purification process. The enzyme was then subjected to successive chromatographic steps, including hydrophobic interaction chromatography on Phenyl-Sepharose, size-exclusion chromatography using Sephacryl S100 (Cytiva, Marlborough, MA, USA), and ion-exchange chromatography on DEAE-Toyopearl. This multi-step process resulted in a highly purified peroxidase with a specific activity of 6170 U/mg. Similarly, PODs from the leaves of guinea grass have been isolated and partially purified using a biphasic polymer system consisting of polyethylene glycol (PEG) and ammonium sulfate [26]. This method allowed for an efficient separation of peroxidase from other proteins, followed by size-exclusion chromatography and ultracentrifugation to obtain a highly active and homogeneous enzyme preparation. In another approach, sweet potato peels were utilized as a POD source [20]. The purification protocol involved homogenization, removal of pigments, and subsequent chromatographic steps using Phenyl-Sepharose and DEAE-Toyopearl columns. This method produced sweet potato peroxidase (SPP) of high purity. Figure 3 shows a schematic representation of the basic stages in the purification of PODs extracted from Colombian plants. These methods underscore the versatility of purification strategies for plant PODs, highlighting the success of using both traditional and innovative techniques to achieve highly purified enzyme preparations from diverse plant sources.
While the protocols described above have been successful in isolating highly active peroxidases from Colombian plant sources, each approach presents distinct advantages and limitations that must be considered when selecting a purification strategy. For instance, traditional precipitation methods, such as ammonium sulfate fractionation, are low-cost and simple to implement, making them suitable for small-scale laboratory extractions. However, they often result in moderate enzyme yield and can cause partial loss of enzymatic activity due to protein denaturation during salt removal steps. Chromatographic techniques, including hydrophobic interaction, ion-exchange, and size-exclusion chromatography, offer high specificity and purity, as demonstrated for royal palm and sweet potato PODs. Nevertheless, they are time-consuming, require specialized equipment, and may have limited scalability for industrial applications. Biphasic polymer systems, such as PEG/ammonium sulfate partitioning, have shown promise for Guinea grass peroxidase, providing a higher yield and preserving enzyme stability by minimizing exposure to harsh conditions. Despite these benefits, polymer-based systems can be costly and generate waste streams that require proper management. Furthermore, the choice of method directly impacts the long-term stability of the enzyme, which is critical for biosensor fabrication and industrial catalysis. Future efforts should focus on developing integrated purification workflows that balance yield, purity, cost, and environmental sustainability, potentially incorporating green extraction techniques and continuous processing to facilitate large-scale production. Table 2 illustrates the main extraction and purification techniques of Colombian plant PODs.

3.3. Biochemical Properties

PODs are versatile enzymes with biochemical properties influenced by pH, temperature, and substrate specificity, which are critical for their functionality in various applications [48]. Typically, PODs exhibit optimal activity in slightly acidic to neutral pH ranges, generally between pH 4 and 7, though some can function in broader pH conditions depending on their source. Temperature stability is another key factor, as most PODs maintain stability and high activity at moderate temperatures (25–45 °C), but their activity may diminish, or enzymes can denature at higher temperatures. Additionally, substrate specificity is a defining characteristic of PODs, as they catalyze reactions involving hydrogen peroxide with various electron donor substrates such as phenols, aromatic amines, and certain organic compounds, though preference varies across enzyme types [49]. Understanding these general properties provides a foundation for examining the unique biochemical traits of PODs derived specifically from Colombian plants, which may offer novel or enhanced attributes.
Table 3 highlights the pH and temperature optimum, inactivation constants, and substrate specificity for PODs derived from six plant sources: royal palm, African oil palm, Guinea grass, lemongrass, sweet potato, sleepy plant, and horseradish. Each enzyme’s unique characteristics underscore the diversity in PODs’ biochemical profiles and offer practical information for selecting specific PODs based on environmental stability and target substrate compatibility. A key observation in the table is the significant variability in the pH optima of these PODs. While many of the PODs demonstrate optimal activity in a broad range of pH values (for instance, African oil palm POD operates effectively from pH 4.0 to 9.0), others, such as sleepy plant POD, show a narrower optimal pH of 4.0. This range of pH adaptability indicates that these enzymes are well-suited for environments with fluctuating or extreme pH conditions, broadening the potential for POD applications across different industrial process. Horseradish peroxidase (HRP), commonly used as a benchmark enzyme, has a pH optimum between 6.0 and 6.5, restricting its usage in acidic conditions. By contrast, the broader pH stability of PODs like those from royal palm and African oil palm could offer enhanced versatility, particularly in biochemical processes where pH stability is a critical factor. Temperature stability, represented by the temperature optimum and inactivation constants, also varies across the POD sources. Notably, royal palm POD exhibits an impressive temperature optimum of 90 °C, significantly higher than that of HRP (25–30 °C). This high thermal tolerance makes it a promising candidate for applications in high-temperature environments, such as industrial catalysis or bioremediation in warmer climates. African oil palm and Guinea grass PODs, with optima at 72 °C and 66 °C, respectively, also show good thermal resilience, although slightly less than royal palm POD. Inactivation constants provide additional insight into thermal stability, with African oil palm and HRP showing relatively low inactivation rates (2.0 × 10−3 and 1.0 × 10−3 min−1, respectively), indicating a slower rate of enzyme denaturation under prolonged exposure to heat. However, the higher inactivation constant of royal palm POD (1.5 × 10−2 min−1) suggests that while it withstands high temperatures, its activity may decrease more quickly over time at these temperatures compared to HRP. Substrate specificity is another critical factor for enzyme selection, as it determines the types of reactions each POD can facilitate. All the PODs in the table show activity toward multiple substrates, with common electron donors like ABTS, ferulic acid, guaiacol, and o-dianisidine. Royal palm, African oil palm, and sweet potato PODs exhibit specificity for ferulic acid, which is valuable in phenolic compound oxidation processes often needed in environmental applications such as pollutant degradation. Lemongrass, Guinea grass, and HRP show specificity for guaiacol and o-dianisidine, indicating their suitability for different types of redox reactions commonly used in biosensing and diagnostic applications. HRP, well-known for its versatility, reacts efficiently with both ABTS and o-dianisidine, but its more limited stability under high temperatures makes it less suitable for high-temperature applications despite its broad substrate compatibility.
Beyond pH, temperature, and substrate specificity, understanding the kinetic behavior of peroxidases is essential for predicting their catalytic performance in different applications. Key kinetic parameters such as Km (Michaelis constant) and Vmax (maximum reaction velocity) provide insights into the affinity between the enzyme and its substrates. For instance, SPP has been reported with Km values ranging from 0.12 to 0.20 mM for substrates such as ABTS and o-phenylenediamine, indicating a high substrate affinity [20]. In comparison, GGP shows slightly higher Km values (0.30–0.45 mM), which correlates with its broader specificity but lower catalytic efficiency [26]. These parameters are critical for the design of biosensors where rapid and specific substrate turnover is desired. The structural stability of Colombian plant PODs has also been a topic of interest due to their ability to withstand extreme conditions. For example, royal palm peroxidase maintains over 80% of its activity at 90 °C, exhibiting a half-life of 50 min under these conditions [32]. Similarly, African oil palm peroxidase demonstrates stability across a wide pH range (4.0–9.0), which is advantageous for industrial processes involving variable reaction environments [19,33]. Such stability profiles are crucial for enzyme immobilization in biosensors and for repeated use in continuous industrial processes. Another important property is the redox potential (E°’) of the heme active site, which determines the enzyme’s ability to catalyze oxidative reactions. Colombian PODs, such as royal palm and GGP, display redox potentials between +0.85 and +0.92 V vs. Ag/AgCl, values comparable to HRP [44,48]. A higher redox potential allows these enzymes to oxidize a broader range of phenolic and aromatic amine substrates, expanding their application in pollutant degradation and biosensing technologies. The integration of kinetic data, structural stability, and redox properties provides a holistic understanding of these enzymes, allowing for the rational selection of peroxidases for specific biotechnological applications and guiding future protein engineering efforts.

4. Biotechnological Applications of Peroxidases

4.1. Electrochemical Biosensing

Electrochemical biosensing is a powerful approach for detecting H2O2 and other analytes of biomedical and environmental significance [51,52,53]. A central element in this method is the use of PODs sourced from plants, which can catalyze reactions involving H2O2, producing signals measurable Via electrochemical techniques. Plant-derived PODs are ideal for biosensors due to their efficiency in redox reactions, stability under various environmental conditions, and natural availability. They catalyze the oxidation of hydrogen peroxide, producing measurable electrochemical signals that correlate with H2O2 concentration. This ability is especially valuable, as H2O2 plays crucial roles in cellular signaling and oxidative stress in biomedical fields, and it also acts as a key pollutant indicator in environmental monitoring [49].
Electrochemical biosensors work by transducing a biochemical interaction into a readable electronic signal, typically using a working electrode modified with a biorecognition element, such as plant POD, that interacts specifically with the analyte of interest. In the case of H2O2, the enzyme’s active site catalyzes its decomposition, triggering electron transfer between the analyte and electrode surface. This interaction yields a current or voltage change, providing a quantifiable measure of H2O2 levels. Notably, the specificity and sensitivity of plant PODs make them versatile for designing biosensors tailored for both clinical and environmental applications. This process is beneficial because it enables low-cost, efficient, and eco-friendly monitoring of H2O2, providing valuable insights into various medical conditions like inflammation, cancer, and cardiovascular diseases, which are often linked to oxidative stress and cellular damage associated with abnormal H2O2 levels [54]. Beyond H2O2 detection, plant-derived peroxidases have shown significant potential for detecting other biologically and environmentally relevant analytes. For instance, they can be engineered to sense glucose, cholesterol, and uric acid, analytes critical for metabolic health monitoring. In glucose sensing, peroxidase enzymes facilitate the oxidation of glucose in the presence of H2O2, producing signals that allow for highly sensitive glucose measurement, an essential function in managing diabetes [55]. Likewise, cholesterol detection is possible through reactions catalyzed by PODs, enabling precise monitoring of lipid levels in blood and contributing to cardiovascular disease prevention. For environmental monitoring, POD-based sensors can detect phenolic compounds, nitrates, and heavy metals in water and soil samples [56]. Phenolic compounds, for instance, are industrial pollutants harmful to aquatic and soil ecosystems, and their detection is crucial for safeguarding environmental health.
Table 4 summarizes the performance of plant-derived POD enzymes immobilized on various electrode materials for electrochemical sensing of H2O2. Each plant POD demonstrates unique sensing characteristics based on its enzyme properties and electrode interface, impacting the detection limits and linear range suitable for H2O2 monitoring in biomedical and environmental applications. Among the PODs, the sleepy plant shows the lowest detection limit of 0.4 µM, achieved using gold nanoparticle-modified electrodes. This superior sensitivity is likely due to the excellent conductivity and high surface area of gold nanoparticles, which facilitate efficient electron transfer between the enzyme and the electrode surface. Gold nanoparticles also provide a stable platform for enzyme immobilization, reducing signal loss and improving sensor sensitivity. Consequently, MPP, combined with gold nanoparticles, may be highly advantageous for detecting low H2O2 concentrations in sensitive biomedical applications, such as monitoring oxidative stress markers in biological samples. Other plant sources, such as lemongrass and horseradish, also demonstrate relatively low detection limits (50 µM), though they utilize graphene and carbon paste electrodes, respectively. Graphene’s high electron conductivity and large surface area contribute to this performance, enhancing electron transfer and enzyme stability on the electrode surface [57,58]. HRP, immobilized on a carbon paste electrode, displays a broader linear range of 0.05–10 mM, making it suitable for applications requiring a wider dynamic range, such as environmental pollutant detection or food safety monitoring. In contrast, royal palm and guinea grass PODs show higher detection limits of 87 µM and 150 µM, respectively, when immobilized on graphene or graphene-chitosan composite electrodes [59]. While graphene enhances electron transfer, the chitosan component may introduce some steric hindrance or diffusional limitations, affecting sensitivity. Despite this, chitosan’s biocompatibility and film-forming properties make it an effective matrix for enzyme immobilization, potentially improving enzyme stability and reusability. The linear range of 0.1–5 mM for royal palm and 0.1–3.5 mM for GGP sensors suggests that they are best suited for environmental applications where H2O2 concentrations are generally higher [26]. SPP on graphene oxide has the highest detection limit (460 µM) among the sensors, which might be attributed to the material’s functional groups. These groups enable strong enzyme binding, but their hydrophilicity can sometimes reduce electron transfer efficiency compared to more conductive materials like pure graphene or gold. This setup has a linear range of 0.25–5 mM, indicating that while sweet potato peroxidase sensors may be less suitable for ultra-trace H2O2 detection, they still hold promise for environmental or industrial monitoring, where a higher detection threshold is acceptable.
PODs, often harnessed for H2O2 detection, exhibit a broad range of catalytic capabilities, positioning them as promising tools for detecting additional analytes, such as triclosan (TCS) [60] and pathogenic bacteria like Staphylococcus aureus [61], a prevalent antimicrobial agent. Thus, PODs can facilitate its degradation, making them valuable for monitoring TCS residues in water sources. A recent study demonstrated the amperometric detection of TCS using screen-printed carbon nanotube electrode modified with GGP. The system exhibited a redox potential of 370 mV and a linear response range from 20 μM to 80 μM and a limit of detection (LOD) of 3 μM, highlighting its potential utility in environmental analysis and food quality control applications. Furthermore, plant PODs hold potential for bacterial detection, especially targeting Staphylococcus aureus, a major cause of hospital-acquired infections. A novel approach employed GGP to detect Staphylococcus aureus in milk samples [61]. This approach involved modifying a screen-printed gold electrode with cysteine and GGP, enabling sensitive electrochemical detection through H2O2 reduction. The modified electrode successfully detected S. aureus in milk within a concentration range of 3 × 102 to 3 × 108 CFU/mL, achieving a detection limit as low as 102 CFU/mL and a rapid response time of around 20 min.
Compared to the commercial standard HRP, Colombian plant-derived PODs offer several unique advantages for biosensor development. For example, RPP exhibits exceptional thermal stability, maintaining activity at temperatures up to 90 °C, which is considerably higher than HRP’s optimal range of 25–30 °C [32,50]. This property is particularly advantageous for sensors operating in harsh environmental or industrial conditions. Similarly, MPP demonstrates ultra-low detection limits when combined with gold nanoparticles (LOD = 0.4 µM), outperforming HRP-based systems in sensitive biomedical applications such as monitoring oxidative stress biomarkers. Additionally, the broad pH tolerance observed in AOP (pH 4.0–9.0) provides flexibility for sensors used in variable sample matrices, such as environmental monitoring or food safety testing. These characteristics highlight the potential of Colombian PODs as cost-effective, locally sourced alternatives that can surpass HRP in performance under specific application conditions.

4.2. Synthesis of Polyaniline

PANI is among the most thoroughly studied conducting polymers, renowned for its remarkable environmental stability and favorable electronic characteristics. Its versatility opens up numerous possibilities for applications, including organic lightweight batteries, light-emitting diodes, optical displays, anticorrosive coatings, and bioanalytical systems [15].
Emeraldine polyaniline exists in two forms: the non-conductive base and the conductive salt form. The salt is produced through the protonation of the imine sites in the emeraldine base using strong acids like organic sulfonic and phosphoric acids, a process known as “doping.” Although doped PANI exhibits conductivity, it suffers from poor solubility in common solvents, limiting its processability [62]. However, PANI can form polyelectrolyte complexes by interacting with soluble polymers that carry negatively charged groups, resulting in stable dispersions of nanoparticles in aqueous media, which enhances processability. In these complexes, PANI typically adopts a doped and chiral state due to interactions between its imine groups and the polymeric anions. These polyelectrolyte complexes can be synthesized through chemical or enzymatic methods. Chemical polymerization of aniline monomers occurs under strongly acidic conditions, usually with 1 M HCl or H2SO4, using ammonium persulfate as the oxidant. The synthesis of PANI complexes can be achieved under environmentally friendly, kinetically controlled conditions using horseradish peroxidase (HRP) as a catalyst. However, HRP exhibits low stability at pH levels below 4.5, which coincides with the pH range suitable for forming polyelectrolyte complexes with negatively charged polymers [45]. To address this issue, alternative PODs that can efficiently polymerize aniline in acidic conditions have been explored, as demonstrated in a study that use RPP for the synthesis of conducting polyelectrolyte complexes of PANI [62,63]. The polymerization of aniline was conducted at pH 2.0 and UV-vis-NIR absorption and EPR techniques confirmed the formation of an electroactive complex similar to traditionally doped PANI. Thus, the thermostable RPP is an efficient catalyst for the polymerization of aniline to obtain PANI complexes under green conditions [64].

4.3. Chemiluminescence Assays

Chemiluminescence (CL) assays are analytical techniques that harness light emission from chemical reactions to detect and quantify various molecules with exceptional sensitivity [65,66]. In these assays, a chemiluminescent substrate, such as luminol, undergoes an oxidation reaction catalyzed by an enzyme like POD in the presence of an oxidizing agent (often hydrogen peroxide), resulting in the release of light. This emitted light is captured by sensitive detectors, with the intensity directly proportional to the concentration of the target analyte. Due to their high sensitivity and low background noise, chemiluminescence assays are commonly used in clinical diagnostics, environmental monitoring, and food safety testing, where they facilitate the detection of low-abundance molecules, pathogens, or specific biomarkers. Compared to fluorescence or colorimetric assays, chemiluminescence assays offer advantages such as reduced interference from background signals and enhanced detection limits. However, these assays require careful optimization of reaction conditions (e.g., pH, temperature, and reagent concentrations) to maximize light yield and maintain enzyme stability, factors that can impact assay reproducibility and performance [65].
HRP-catalyzed CL is a widely used method for detecting low concentrations of analytes due to its high sensitivity and low background signal [67]. HRP is commonly used to catalyze the oxidation of luminol or other substrates in the presence of hydrogen peroxide, which produces light detectable by photomultiplier tubes or other light-sensitive devices. This light output is proportional to the concentration of the target analyte, making HRP-based CL assays particularly useful in immunoassays, DNA detection, and various biochemical analyses [68]. However, despite its popularity, HRP has several limitations. One significant disadvantage is its sensitivity to environmental conditions, such as pH and temperature; HRP can quickly lose activity outside of its optimal pH range (around pH 7) or under high temperatures, which limits its utility in harsh or variable assay conditions.
POD from African oil palm, for example, has demonstrated potential for enhanced stability and reactivity in specific pH and temperature ranges, which can be advantageous for assays requiring durability under varying conditions [69]. Studies indicate that this enzyme can withstand higher temperatures compared to HRP, making it a valuable alternative for applications where thermal stability is essential. Meanwhile, POD from the royal palm offers distinct advantages in terms of substrate affinity, particularly with substrates like 3,3′,5,5′-tetramethylbenzidine (TMB) and luminol [70]. The efficiency of these enzymes is affected by factors such as ionic strength, pH, and the presence of cofactors, which influence their conformational state and active site accessibility, thereby impacting their chemiluminescent output. Optimizing these conditions can yield stronger luminescent signals, enhancing assay sensitivity.
While HRP remains the most widely used enzyme in chemiluminescence (CL) assays, its activity declines sharply under extreme pH or elevated temperatures, limiting its robustness. In contrast, Colombian PODs such as RPP retain over 80% activity at pH 3 and 90 °C, providing a more stable catalytic platform for CL systems exposed to variable reaction environments [32,69]. This increased stability reduces assay variability and enhances reproducibility, making these enzymes suitable for low-cost diagnostic kits in regions where controlled laboratory conditions may not be feasible.

4.4. Cross-Linked Enzymatic Aggregates

CLEAs are innovative biocatalytic materials formed by aggregating enzymes through precipitation, followed by cross-linking to create stable, insoluble enzyme clusters [16]. This approach enhances enzyme stability and reusability, making CLEAs valuable for applications in industrial biocatalysis, environmental remediation, and biosensing. Unlike conventional enzyme immobilization, CLEAs do not require a solid support, which simplifies the process and reduces production costs. CLEAs are applied in fields where enzymes must withstand harsh conditions, including organic synthesis, wastewater treatment, and biotransformation of complex substrates [71].
When CLEAs are synthesized with PODs, they offer further benefits for oxidative reactions. Peroxidase-CLEAs can be used in chemiluminescence assays, biosensors for detecting hydrogen peroxide, and pollutant degradation, where they catalyze oxidation reactions with improved stability under extreme pH, temperature, or organic solvents. This stability is crucial for long-term, repeated use in bioelectrochemical sensors and diagnostic kits, enhancing their efficiency and cost-effectiveness.
HRP has been extensively used to form CLEAs due to its high catalytic activity and compatibility with a variety of substrates. However, HRP-CLEAs have limitations, including sensitivity to denaturation under extreme conditions like high temperatures or fluctuating pH levels, which can reduce enzyme activity over time [72]. These factors have driven interest in exploring alternative peroxidase sources that could provide greater resilience and cost efficiency. To address these limitations, researchers are investigating plant-derived peroxidases from species like the RPP and GGP. For example, RPP was subject to a study focus in its immobilization through CLEAs to enhance its stability and activity. The resulting RPTP-CLEAs showed remarkable activity, maintaining 40% of maximum activity even at pH 3, where free RPTP is inactive. In thermal stability tests, the RPTP-CLEAs retained high stability similar to the free enzyme, with a half-life of 50 min at 90 °C and pH 7. Unlike the free enzyme, which undergoes subunit dissociation at pH 3, RPTP-CLEAs avoided this instability, showing significant thermostabilization [73]. Additionally, RPTP-CLEAs also exhibited good stability with low hydrogen peroxide concentrations (10 mM), though stability declined at higher concentrations (300 mM), where immobilization provided limited improvement. In practical applications, the RPTP-CLEAs were effective in decolorizing methyl orange using 5 mM hydrogen peroxide for four cycles (4 h each) without noticeable activity loss, achieving around 50% substrate degradation. With 225 mM hydrogen peroxide, activity gradually decreased across cycles but allowed complete colorant degradation [72]. These findings suggest that RPTP-CLEAs can function under challenging conditions, such as pH 3 and high hydrogen peroxide levels, where the free enzyme would typically be inactive, supporting their potential use in various industrial and environmental applications.
But not only was RPTP studied; GGP was also investigated for immobilization through CLEAs for the decolorization of indigo carmin (IC) [74]. The biocatalyst was prepared using 50% v/v ethanol and 0.88% w/v glutaraldehyde, with stirring for 1 h, achieving an immobilization yield of 93.74% and a specific activity of 36.75 U mg−1. This immobilized form demonstrated 61% higher activity than the free enzyme at its optimal pH (pH 6 for both), with activity levels nearly 10 times higher at a pH of 9. GGP-CLEAs also showed significantly greater thermal stability, with improvements of 2–4 times compared to the free enzyme, and were 2–3 times more resistant to hydrogen peroxide. The GGP-CLEAs effectively removed over 80% of 0.05 mM indigo carmine at pH 5 in the presence of 0.55 mM H2O2 after 60 min, outperforming the free enzyme. However, operational stability tests indicated a reduction in enzyme activity of over 60% after 4 cycles, likely due to suicide inhibition [74].
These PODs offer potentially more sustainable, cost-effective, and environmentally resilient alternatives for CLEA applications. Studies suggest that PODs from these plants exhibit stability across a broader range of environmental conditions, which can be advantageous for applications requiring robust catalytic activity in varied settings. By creating CLEAs with RPP and GGP, it may be possible to develop biocatalysts that maintain high efficiency and stability in applications like biosensors, pollutant degradation, and chemiluminescent assays while reducing dependency on traditional HRP sources.
Colombian PODs also demonstrate superior performance when incorporated into CLEAs compared to traditional HRP. For instance, RPP-CLEAs maintained high activity across four decolorization cycles at pH 3, a condition under which free HRP and HRP-CLEAs would typically lose activity [73]. Similarly, GGP-CLEAs displayed 2–3 times greater resistance to hydrogen peroxide inactivation than free enzymes or HRP-CLEAs, making them more suitable for industrial wastewater treatment and other challenging oxidative processes [74]. These findings emphasize the potential of Colombian PODs to serve as resilient, sustainable alternatives for industrial biocatalysis while reducing dependency on imported HRP.
While CLEAs significantly improve enzyme stability and reusability compared to free enzymes, several limitations remain. One key challenge is operational stability, as repeated reaction cycles often result in gradual activity loss due to partial enzyme inactivation or structural degradation of the aggregates. For example, GGP-CLEAs exhibited a >60% reduction in activity after four cycles of indigo carmine degradation, likely caused by suicide inactivation in the presence of excess hydrogen peroxide [74]. Similarly, RPP-CLEAs, while stable at low H2O2 concentrations, showed diminished stability under high oxidative stress, limiting their long-term utility in industrial processes [73]. Another important issue is recyclability, which directly impacts process economics and environmental sustainability. Although CLEAs are theoretically reusable, repeated recovery steps may cause physical losses or partial fragmentation of the aggregates, reducing their effectiveness over time. This highlights the need for strategies to enhance mechanical robustness and improve immobilization methods. To address these limitations, advanced engineering approaches should be considered. Protein engineering through site-directed mutagenesis or directed evolution could generate POD variants with higher intrinsic resistance to oxidative stress and extreme pH or temperature conditions. Additionally, integrating PODs with nanozymes—nanomaterials with enzyme-mimicking activity—offers a promising hybrid strategy. For instance, coupling PODs with graphene oxide or metal nanoparticles could enhance electron transfer, improve stability, and provide self-regenerative catalytic activity, thus extending the functional lifespan of the biocatalyst [24,57]. These hybrid CLEA-nanozyme systems could also enable multifunctionality, combining biocatalytic specificity with the robustness of inorganic materials. Future research should focus on scalable, green synthesis approaches for these hybrid systems to ensure environmental compatibility and economic feasibility.

5. Sustainability and the Circular Bioeconomy in the Context of Colombian Plants Peroxidases

Sustainability and the circular bioeconomy provide the conceptual framework for POD valorization in Colombia. Agricultural by-products such as palm fronds, guinea grass leaves, or sweet potato peels are abundant and frequently discarded. Their repurposing into enzyme sources reduces waste while generating added value. This approach aligns with the Sustainable Development Goals (SDGs), particularly responsible production, climate action, and innovation in green technologies [10,74,75,76].
The valorization of Colombian agricultural by-products for POD extraction not only contributes conceptually to the circular bioeconomy but also yields quantifiable environmental benefits. For instance, Colombia generates an estimated 3.5–4.0 million tons of agricultural residues annually, with a significant proportion coming from crops such as sugarcane, palm oil, and tubers like sweet potato [13,30]. Repurposing even 10% of these residues for biotechnological processes could prevent approximately 350,000 tons of organic waste from being landfilled or burned each year, reducing methane emissions associated with anaerobic decomposition. From a climate perspective, substituting traditional chemical processes or imported commercial enzymes with locally produced PODs offers meaningful CO2 savings. The carbon footprint of industrial enzyme production, primarily HRP derived from horseradish, has been estimated at 8–10 kg CO2 per kilogram of purified enzyme when factoring in cultivation, transportation, and processing [10]. By sourcing PODs from local agricultural waste streams, transportation-related emissions could be reduced by up to 40–50%, while valorizing waste biomass also sequesters carbon that would otherwise be released during open burning. Moreover, POD-based processes, such as wastewater treatment using CLEAs, have demonstrated a 30–45% reduction in chemical oxidant usage compared to conventional treatment methods [11,74]. This translates to lower secondary pollution and reduced energy requirements for chemical production. For example, implementing POD-CLEA systems at a medium-sized textile facility could reduce annual CO2 emissions by 120–150 metric tons, primarily by decreasing the demand for synthetic oxidants like hydrogen peroxide and chlorine compounds. Quantifying these benefits provides a clearer perspective on how Colombian POD-based biotechnologies can move beyond laboratory-scale innovation to become measurable contributors to sustainability goals, including the United Nations Sustainable Development Goals (SDGs 12 and 13).

6. Conclusions

The valorization of Colombian agricultural by-products for POD extraction offers a powerful pathway to sustainable biotechnological innovation. This review highlights how plant-derived PODs can be harnessed for diverse applications, including biosensing, advanced material synthesis, environmental remediation, and health monitoring while reducing waste and supporting local economies.
Looking ahead, three main research priorities emerge:
(i)
Scaling up POD production: Future studies should focus on optimizing extraction and purification methods for large-scale, cost-effective production. This includes developing continuous processing technologies, green extraction approaches, and robust immobilization strategies to meet industrial demands.
(ii)
Structural characterization: Detailed studies using X-ray crystallography, cryo-EM, and computational modeling are needed to understand the structural basis of the exceptional thermal stability and substrate specificity of Colombian PODs. These insights will enable rational protein engineering and design of tailored biocatalysts.
(iii)
Integration into circular bioeconomy policies: Collaboration with policymakers, industries, and local communities is essential to incorporate POD-based technologies into Colombia’s circular bioeconomy framework, promoting sustainable waste valorization and contributing to national and global climate action goals.
By advancing these research areas, Colombian plant PODs can transition from laboratory-scale innovations to impactful technologies, fostering environmental sustainability, economic growth, and global leadership in green biotechnology.

Funding

This research was funded by [Vicerrectoría de Investigaciones, Universidad Industrial de Santander] grant number [3923].

Acknowledgments

We would like to acknowledge the Universidad Industrial de Santander for financial support.

Conflicts of Interest

The author declares no conflicts of interest.

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Processes 13 03198 g001
Figure 1. Novel biotechnological applications of Colombian plant-derived PODs from agricultural by-products, emphasizing their use in biosensing, advanced materials, and environmental remediation.
Figure 1. Novel biotechnological applications of Colombian plant-derived PODs from agricultural by-products, emphasizing their use in biosensing, advanced materials, and environmental remediation.
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Figure 2. Main Colombian plant sources of PODs with high potential for sustainable enzyme production.
Figure 2. Main Colombian plant sources of PODs with high potential for sustainable enzyme production.
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Figure 3. Stepwise protocol for POD extraction and purification from Colombian plants, illustrating innovative approaches that improve stability and scalability for biotechnological applications.
Figure 3. Stepwise protocol for POD extraction and purification from Colombian plants, illustrating innovative approaches that improve stability and scalability for biotechnological applications.
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Table 1. Comparison of peroxidase activity across plant parts (adapted from [31]).
Table 1. Comparison of peroxidase activity across plant parts (adapted from [31]).
Plant PartSource of PODPOD Activity (U/g)
FruitsAlmond (Terminalia catappa)<1.0
Cocoa (Theobroma cacao)11.6
Coffee (Coffea arabica)22.9
Cocoa palm (Cocos nucifera)1.2
Tree tomato (Cyphomandra betacca)16.2
Totumo (Crescentia cujete)5.8
RootsCelery (Apium graveolens)58.0
Arracacha (Arracacia xanthorrhiza)<1.0
Sweet potato (Ipomea batatas)1800.0
Coriander (Coriandrum sativum)35.0
Bore (Colocasa esculenta)370.0
Ginger (Zingeber officinale)11.6
Red radish (Rapharus sativas)121.3
Horseradish (Armoracia rusticana)2600.0
Cassava (Manihot esculenta)1.7
LeavesOleander (Nerium oleander)98.3
Pear cactus (Monstera delisiosa)179.0
Banana (Musa sapientum)49.7
Bamboo (Bambusa guadua)<1.0
Spanish moss (Tillandsia recurvata)5.2
Boojum tree (Cereus hexagonus)19.0
Marigold (Calendula oficionales)231.2
Bottlebrush (Callistemon lanceolatu)<1.0
Sugar cane (Sacharum officinarum)104.0
Sleepy plant (Mimosa pudica)460.0
Fique (Agave fourcroides)19.6
Fern (Adiamtum obliguum)<1.0
Castor bean plant (Ricinum communis L.)440.0
Lemongrass (Cymbopogon citratus)390.0
Fan palm (copernica pectori)220.0
African oil palm (eleais guineensis)566.0
Date palm (Phoenix dactilera)580.0
Royal palm (Roystonea regia)694.0
Coconut palm (Cocos nucifera)48.6
Corozo palm (Acrocomia aculeata)570.0
Wine palm (Scheelea butyracea)173.4
Thatch palm (Astrocarium sp.)220.0
Macaw palm (Bactris sp.)196.0
Palma mararai (Aiphanes cariotifolia)1145.0
Guinea Grass (Panicum maximum)980.0
Parsley (Petroselinum sativum)35.0
Table 2. Summary of extraction and purification techniques of Colombian plant peroxidases, including yield, advantages, limitations, and main biotechnological applications.
Table 2. Summary of extraction and purification techniques of Colombian plant peroxidases, including yield, advantages, limitations, and main biotechnological applications.
Plant SourceExtraction TechniqueYield/Specific
Activity		AdvantagesDrawbacksApplications
Royal palm
(Roystonea regia)		Homogenization → Ammonium sulfate precipitation → Hydrophobic interaction + ion-exchange chromatography6170 U/mg [32]High purity, excellent thermal stabilityTime-consuming, high cost, not easily scalableElectrochemical biosensors, high-temperature industrial catalysis
Guinea grass
(Panicum maximum)		Biphasic polymer system (PEG/ammonium sulfate) → Size-exclusion chromatography2000–3000 U/mg [26]Good stability preservation, moderate costPolymer disposal issues, requires optimizationBiosensors for H2O2, environmental monitoring
Sweet potato
(Ipomea batatas)		Homogenization → Pigment removal → Hydrophobic interaction + ion-exchange chromatography1800 U/mg [20]High substrate specificity, compatible with food industryModerate yield, pigment interference can complicate extractionFood biosensors, wastewater treatment
African oil palm
(Elaeis guineensis)		Homogenization → Ammonium sulfate precipitation → Chromatographic purification2500 U/mg [33]Good thermal stability, wide pH toleranceLimited studies on scalabilityEnvironmental remediation, CLEA synthesis
Lemongrass
(Cymbopogon citratus)		Aqueous extraction → Ammonium sulfate precipitation → Chromatography1200 U/mg [34]Easy implementation, accessible raw materialEnzyme unstable at pH > 7Biosensors for H2O2 and phenolic compounds
Sleepy plant
(Mimosa pudica)		Aqueous extraction → Ammonium sulfate precipitation → DEAE-Toyopearl chromatography460 U/mg [38]Very low detection limit with gold electrodesNarrow pH stability rangeBiosensors for sensitive biomedical detection
Table 3. Comparative biochemical properties of peroxidases from Colombian plants.
Table 3. Comparative biochemical properties of peroxidases from Colombian plants.
PODs SourcepH OptimumTemperature Optimum (°C)Inactivation Constant (min−1)Substrate SpecificityReference
Royal palm7.0–9.0901.5 × 10−2Ferulic acid
ABTS		[32]
African oil palm4.0–9.0722.0 × 10−3Ferulic acid
ABTS		[19]
Guinea grass7.0–9.0668.0 × 10−3Guaiacol
ABTS
o-dianisidine		[26]
Lemongrass4.0–6.0661.0 × 10−2Guaiacol
o-dianisidine		[34]
Sweet potato8.0607.0 × 10−3Ferulic acid
ABTS
o-Phenylene diamine		[20]
Sleepy plant4.0557.0 × 10−3-[38]
Horseradish6.0–6.525–301.0 × 10−3o-dianisidine
ABTS		[50]
Table 4. Comparison of Plant-Derived Peroxidase-Based Electrochemical Sensors for Hydrogen Peroxide Detection.
Table 4. Comparison of Plant-Derived Peroxidase-Based Electrochemical Sensors for Hydrogen Peroxide Detection.
Plant SourceElectrode MaterialDetection Limit (μM)Linear Range (mM)Reference
Royal palmGraphene/chitosan870.1–5[59]
Guinea grassGraphene1500.1–3.5[26]
LemongrassGraphene500.5–4[49]
Sweet potatoGraphene oxide4600.25–5[20]
Sleepy plantGold nanoparticles0.40.5–5[37]
HorseradishCarbon paste500.05–10[48]
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Castillo, J.J. From Waste to Wonder: Valorization of Colombian Plant By-Products for Peroxidase Production and Biotechnological Innovation. Processes 2025, 13, 3198. https://doi.org/10.3390/pr13103198

AMA Style

Castillo JJ. From Waste to Wonder: Valorization of Colombian Plant By-Products for Peroxidase Production and Biotechnological Innovation. Processes. 2025; 13(10):3198. https://doi.org/10.3390/pr13103198

Chicago/Turabian Style

Castillo, John J. 2025. "From Waste to Wonder: Valorization of Colombian Plant By-Products for Peroxidase Production and Biotechnological Innovation" Processes 13, no. 10: 3198. https://doi.org/10.3390/pr13103198

APA Style

Castillo, J. J. (2025). From Waste to Wonder: Valorization of Colombian Plant By-Products for Peroxidase Production and Biotechnological Innovation. Processes, 13(10), 3198. https://doi.org/10.3390/pr13103198

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