Search Results (65)

Environmental and economic concerns due to the increasing use of fossil-based chemicals, especially fuel, may be alleviated by production of renewable fuels based on plant biomass, in particular, waste. Multistep cascades of enzymatic reactions are being increasingly sought to enhance the effectiveness of sustainable, environment-friendly processes. The biochemical transformation of lignocellulosic biomass and oils into fatty acid esters (“biodiesel”) involves biomass pretreatment, followed by polysaccharide hydrolysis and sugar fermentation to alcohol, either sequentially or simultaneously. Subsequent trans-esterification with waste or non-food-based oils is usually carried out in an organic solvent. Biocatalysis in aqueous emulsion offers significant advantages. This study presents a novel “one-pot” emulsion-based process for transforming unmodified cellulose and castor oil into biodiesel via hybridized yeasts with cellulose-coated micro-particles incorporating cellulolytic enzymes and lipases. The resultant consolidated bioprocess of saccharification, fermentation, and transesterification (cSFT) promotes effective substrate channeling and can potentially serve as a model for emulsion-based “one-pot” transformations of cellulose into valuable chemicals. Full article

Biocatalysis is fundamental to biological processes and sustainable chemical productions. Over time, the biocatalysis strategy has been widely researched. Initially, biomanufacturing and catalysis of high-value chemicals were carried out through direct immobilization and application of biocatalysts, including natural enzymes and living cells. With the evolution of green chemistry and environmental concern, hybrid photoelectro-biocatalysis (HPEB) platforms are seen as a new approach to enhance biocatalysis. This strategy greatly expands the domain of natural biocatalysis, especially for bio-based components. The selective valorization of renewable furan derivatives, such as 5-hydroxymethylfurfural (HMF) and furfural, is central to advancing biomass-based chemical production. Biocatalysis offers high chemo-, regio-, and stereo-selectivity under mild conditions compared with traditional chemical catalysis, yet it is often constrained by the costly and inefficient regeneration of redox cofactors like NAD(P)H. Photoelectrocatalysis provides a sustainable means to supply reducing equivalents using solar or electrical energy. In recent years, hybrid systems that integrate biocatalysis with photoelectrocatalysis have emerged as a promising strategy to overcome this limitation. This review focuses on recent advances in such systems, where photoelectrochemical platforms enable in situ cofactor regeneration to drive enzymatic transformations of furan-based substrates. We critically analyze representative coupling strategies, materials and device configurations, and reaction engineering approaches. Finally, we outline future directions for developing efficient, robust, and industrially viable hybrid catalytic platforms for green biomass valorization. Full article

Adamantane is a unique tricyclic hydrocarbon with a rigid, diamond-like structure. It is widely distributed in natural hydrocarbons and has significant potential applications in medicine, materials science, and pharmaceuticals. Despite its high chemical stability, biocatalytic methods using cytochrome P450 enzymes and microorganisms, such as Pseudomonas strains and actinobacteria, demonstrate high regional specificity in the hydroxylation and modification of adamantane, primarily at tertiary C–H bonds. This review summarises the latest data on the mechanisms and pathways of the microbial transformation of adamantane and its derivatives, including the key metabolites and enzymatic systems involved. The advantages of biocatalysis—namely, high selectivity, environmental friendliness and mild reaction conditions—are highlighted as a promising approach to the synthesis of functional adamantane derivatives for use in the development of innovative drugs and materials. The limitations of current methods and prospects for development are also discussed, including searching for new microorganisms and regulating enzymatic activity to increase the efficiency of biotransformation. Full article

Chitin deacetylases (CDAs), which catalyze the deacetylation of chitin to produce chitosan, have garnered significant interest due to their environmental compatibility and ability to control product quality. However, the low conversion efficiency resulting from chitin’s high molecular weight and crystallinity, as well as structural limitations of CDAs, has impeded their industrial application. In this study, we present the integrated approach combining bioinformatics and computational tools (adaptive Poisson–Boltzmann solver, Fpocket, and ProteinPlus) to systematically analyze sequence features and variations in active pocket properties among CDAs from diverse origins. Experimental evaluation of the deacetylation activity of AnCDA, AsCDA, BaCDA, and ScCDA, each with distinct pocket characteristics, on chitin substrates with varying molecular parameters revealed that CDAs with high hydrophobicity scores and low surface-to-volume ratios exhibited superior efficiency in converting high-molecular-weight chitin. These findings guide the rational selection and engineering of CDAs for industrial biocatalysis. Full article

Pectins are high-value plant cell-wall polysaccharides with extensive applications in the food, pharmaceutical, textile, paper, and environmental sectors. Traditional extraction and processing methodologies rely heavily on harsh acids, high temperatures, and non-renewable solvents, generating substantial environmental and economic costs. This review consolidates recent advances across the entire Bacillus–pectinase value chain, from green pectin extraction and upstream substrate characterization, through process and statistical optimization of enzyme production, to industrial biocatalysis applications. We propose a practical roadmap for developing high-efficiency, low-environmental-footprint enzyme systems that support circular bioeconomy objectives. Critical evaluation of optimization strategies, including submerged versus solid-state fermentation, response surface methodology, artificial neural networks, and design of experiments, is supported by comparative data on strain performance, fermentation parameters, and industrial titers. Sector-specific case studies demonstrate the efficacy of Bacillus pectinases in fruit-juice clarification, textile bio-scouring, paper bio-bleaching, bio-based detergents, coffee and tea processing, oil extraction, animal feed enhancement, wastewater treatment, and plant-virus purification. Remaining challenges, including enzyme stability in complex matrices, techno-economic scale-up, and structure-guided protein engineering, are identified. Future directions are charted toward CRISPR-driven enzyme design and fully integrated circular-economy bioprocessing platforms. Full article

Microbial spores are increasingly recognized as multifunctional platforms for enzyme immobilization, combining natural resilience with biotechnological versatility. Their inherent structural complexity enables high enzyme load, thermal and chemical stability, and robustness to be repeatedly used under industrially relevant conditions, largely widening their application scope. This review explores the growing role of spore-based systems in biocatalysis, from naturally active spores to engineered microbial hosts capable of producing immobilized enzymes in situ. Compared to conventional immobilization techniques, spore-based strategies offer simplified workflows, reduced environmental impact, and greater sustainability. Recent innovations also extend beyond traditional applications, introducing artificial spores and incorporating spores into biocomposite materials and biosensors. These developments reflect a shift from basic enzyme stabilization research toward scalable solutions in waste remediation, polymer degradation, green chemistry, and synthetic biology. Overall, spore-enabled biocatalysis represents a modular and robust toolset for advancing industrial biotechnology and sustainable manufacturing, instrumental in achieving a circular and bioeconomy. Full article

Enzymes are highly selective and efficient biological catalysts that play a critical role in modern industrial biocatalysis. Their ability to operate under mild conditions and reduce environmental impact makes them ideal alternatives to conventional chemical catalysts. This review provides a comprehensive overview of advances in enzyme-based catalysis, focusing on enzyme classification, engineering strategies, and industrial applications. The six major enzyme classes—hydrolases, oxidoreductases, transferases, lyases, isomerases, and ligases—are discussed in the context of their catalytic roles across sectors such as pharmaceuticals, food processing, textiles, biofuels, and environmental remediation. Recent developments in protein engineering, including directed evolution, rational design, and computational modeling, have significantly enhanced enzyme performance, stability, and substrate specificity. Emerging tools such as machine learning and synthetic biology are accelerating the discovery and optimization of novel enzymes. Progress in enzyme immobilization techniques and reactor design has further improved process scalability, reusability, and operational robustness. Enzyme sourcing has expanded from traditional microbial and plant origins to extremophiles, metagenomic libraries, and recombinant systems. These advances support the integration of enzymes into green chemistry and circular economy frameworks. Despite challenges such as enzyme deactivation and cost barriers, innovative solutions continue to emerge. Enzymes are increasingly enabling cleaner, safer, and more efficient production pathways across industries, supporting the global shift toward sustainable and circular manufacturing. Full article

Enzyme-based biosensors have emerged as a transformative technology, leveraging the specificity and catalytic efficiency of enzymes across various domains, including medical diagnostics, environmental monitoring, food safety, and industrial processes. These biosensors integrate biological recognition elements with advanced transduction mechanisms to provide highly sensitive, selective, and portable solutions for real-time analysis. This review explores the key components, detection mechanisms, applications, and future trends in enzyme-based biosensors. Artificial enzymes, such as nanozymes, play a crucial role in enhancing enzyme-based biosensors by mimicking natural enzyme activity while offering improved stability, cost-effectiveness, and scalability. Their integration can significantly boost sensor performance by increasing the catalytic efficiency and durability. Additionally, lab-on-a-chip and microfluidic devices enable the miniaturization of biosensors, allowing for the development of compact, portable devices that require minimal sample volumes for complex diagnostic tests. The functionality of enzyme-based biosensors is built on three essential components: enzymes as biocatalysts, transducers, and immobilization techniques. Enzymes serve as the biological recognition elements, catalyzing specific reactions with target molecules to produce detectable signals. Transducers, including electrochemical, optical, thermal, and mass-sensitive types, convert these biochemical reactions into measurable outputs. Effective immobilization strategies, such as physical adsorption, covalent bonding, and entrapment, enhance the enzyme stability and reusability, enabling consistent performance. In medical diagnostics, they are widely used for glucose monitoring, cholesterol detection, and biomarker identification. Environmental monitoring benefits from these biosensors by detecting pollutants like pesticides, heavy metals, and nerve agents. The food industry employs them for quality control and contamination monitoring. Their advantages include high sensitivity, rapid response times, cost-effectiveness, and adaptability to field applications. Enzyme-based biosensors face challenges such as enzyme instability, interference from biological matrices, and limited operational lifespans. Addressing these issues involves innovations like the use of synthetic enzymes, advanced immobilization techniques, and the integration of nanomaterials, such as graphene and carbon nanotubes. These advancements enhance the enzyme stability, improve sensitivity, and reduce detection limits, making the technology more robust and scalable. Full article

This paper reviews the integration of artificial intelligence (AI) and machine learning in biorefineries and bioprocessing, with applications in biocatalysis, enzyme optimization, real-time monitoring, and quality assurance. AI contributes to predictive modeling and allows the precise forecasting of process outcomes, resource management, and energy utilization. AI models, including supervised, unsupervised, and reinforcement learning, support improvements in important bioprocess stages, such as fermentation, purification, and microbial biosynthesis. Digital twins and soft-sensing technologies enable real-time control and increase operational precision in complex bioprocess environments. Hybrid modeling integrates data-driven AI techniques with common scientific principles, improving scalability and adaptability under dynamic operational conditions. This review addresses challenges in AI implementation, such as data standardization, model transparency, and the need for interdisciplinary collaboration. The discussion concludes with future directions and sustainable AI strategies, highlighting the potential of AI to strengthen scalable, efficient, and environmentally sustainable biorefinery operations. These findings highlight how AI-driven methodologies improve operational efficiency, reduce resource waste, and facilitate sustainable innovation in bioprocesses, thereby strengthening sustainability within the bioeconomy. Full article

Biocatalysis is one of the oldest fields that has been used in industrial applications, with one of the earliest purposeful examples being the mass production of acetic acid from an immobilized Acinetobacter strain in the year 1815. Efficiency, specificity, reduced reaction times, lower overall costs, and environmental friendliness are some advantages biocatalysis has over conventional chemical synthesis, which has made biocatalysis increasingly used in industry. We highlight three necessary fields that are fundamental to advancing industrial biocatalysis, including biocatalyst engineering, solvent engineering, and mechanistic engineering. However, the fundamental mechanism of enzyme function is often overlooked or given less attention, which can limit the engineering process. In this review, we describe how mechanistic enzymology benefits industrial biocatalysis by elucidating key fundamental principles, including the k_cat and k_cat/K_m parameters. Mechanistic enzymology presents a unique field that provides in-depth insights into the molecular mechanisms of enzyme activity and includes areas such as reaction kinetics, catalytic mechanisms, structural analysis, substrate specificity, and protein dynamics. In line with the objective of protein engineering to optimize enzyme activity, we summarize a range of strategies reported in the literature aimed at improving the product release rate, the chemical step of catalysis, and the overall catalytic efficiency of enzymes. Further into this review, we delineate kinetic solvent viscosity effects (KSVEs) as a very efficient, cost-effective, and easy-to-perform method to probe different aspects of enzyme reaction mechanisms, including diffusion-dependent kinetic steps and rate-limiting steps. KSVEs are cost-effective because simple kinetic enzyme assays, such as the Michaelis–Menten kinetic approach, can be combined with them without the need for specialized and costly equipment. Other techniques in protein engineering and genetic engineering are also covered in this review. Additionally, we provide information on solvent systems in enzymatic reactions, details on immobilized biocatalysts, and common misconceptions that misguide enzyme design and optimization processes. Full article

Lipases are important industrial enzymes with a wide range of applications across various sectors. Cold-active lipases are particularly well suited for industrial processes that operate at low temperatures (such as food processing and environmental remediation) due to their high catalytic efficiency and energy-saving benefits. In this study, a novel lipase—LipU (GenBank accession: PV094892)—was heterologously expressed from Bacillus cereus U2 and characterized for its low-temperature adaptability and alkaline resistance. LipU belongs to the lipase Subfamily I.5 and shares the highest amino acid sequence identity (53.32%) with known homologs. Enzymatic assays revealed that LipU exhibits optimal activity at 20 °C and pH 11. It retained 95% of its initial activity after 24 h of incubation at 4 °C and pH 11.0. Furthermore, the activity of LipU was enhanced by Ca²⁺, Na⁺, Tween 20, and Tween 80, whereas it was inhibited by Cu²⁺, Zn²⁺, Mn²⁺, and sodium dodecyl sulfate (SDS). LipU demonstrated tolerance to various organic solvents of differing polarity; after 1 h of exposure to 15% (v/v) ethanol, n-butanol, isoamyl alcohol, dimethyl sulfoxide, or glycerol, it retained over 78.6% of its activity. These properties make LipU a promising candidate for industrial applications, including for leather degreasing, alkaline wastewater treatment, and low-temperature biocatalysis. Full article

Oleochemicals, which are obtained from vegetable and animal fats and oils, have become indispensable in the food, cosmetics, pharmaceutical and biofuel industries. Traditionally, they are synthesized using chemical catalysts, a process that is often associated with high energy requirements and a considerable environmental impact. Biocatalysis, using enzymes such as lipases, has emerged as a transformative alternative that offers high specificity, environmental friendliness and cost-efficiency. This review comprehensively examines the current state of biocatalysis for oleochemical synthesis, highlighting key reactions such as esterification and transesterification and their integration into industrial processes. A bibliometric analysis uncovers global trends and collaborations, while case studies illustrate cost efficiency and scalability. The article outlines recommendations and future research directions to advance biocatalytic processes. This review is intended to be an important resource for researchers and industries transitioning to sustainable oleochemical production. Full article

Enzyme immobilization plays a critical role in enhancing the efficiency and sustainability of biocatalysis, addressing key challenges such as limited enzyme stability, short shelf life, and difficulties in recovery and recycling, which are pivotal for green chemistry and industrial applications. Classical approaches, including adsorption, entrapment, encapsulation, and covalent bonding, as well as advanced site-specific methods that integrate enzyme engineering and bio-orthogonal chemistry, were discussed. These techniques enable precise control over enzyme orientation and interaction with carriers, optimizing catalytic activity and reusability. Key findings highlight the impact of immobilization on improving enzyme performance under various operational conditions and its role in reducing process costs through enhanced stability and recyclability. The review presents numerous practical applications of immobilized enzymes, including their use in the pharmaceutical industry for drug synthesis, in the food sector for dairy processing, and in environmental biotechnology for wastewater treatment and dye degradation. Despite the significant advantages, challenges such as activity loss due to conformational changes and mass transfer limitations remain, necessitating tailored immobilization protocols for specific applications. The integration of immobilization with modern biotechnological advancements, such as site-directed mutagenesis and recombinant DNA technology, offers a promising pathway for developing robust, efficient, and sustainable biocatalytic systems. This comprehensive guide aims to support researchers and industries in selecting and optimizing immobilization techniques for diverse applications in pharmaceuticals, food processing, and fine chemicals. Full article