Search Results (73)

In recent decades, there has been a marked surge in the development of marine-by-product-derived ingredients for cosmetic applications, driven by the increasing demand for natural, sustainable, and high-performance formulations. Marine animal by-products, particularly those from fish, crustaceans, and mollusks, represent an abundant yet underutilized source of bioactive compounds with notable potential in cosmeceutical innovation. Generated as waste from the fishery and seafood-processing industries, these materials are rich in valuable bioactives, such as chitosan, collagen, peptides, amino acids, fatty acids, polar lipids, lipid-soluble vitamins, carotenoids, pigments, phenolics, and mineral-based substrates like hydroxyapatite. Marine by-product bioactives can be isolated via several extraction methods, and most importantly, green ones. These compounds exhibit a broad spectrum of skin-health-promoting effects, including antioxidant, anti-aging, anti-inflammatory, antitumor, anti-wrinkle, anti-hyperpigmentation, and wound-healing properties. Moreover, applications extend beyond skincare to include hair, nail, and oral care. The present review provides a comprehensive analysis of bioactives obtained from marine mollusks, crustaceans, and fish by-products, emphasizing modern extraction technologies with a focus on green and sustainable approaches. It further explores their mechanisms of action and documented efficacy in cosmetic formulations. Finally, the review outlines current limitations and offers future perspectives for the industrial valorization of marine by-products in functional and environmentally-conscious cosmetic development. Full article

Peptides are currently vital components in nutrition with physiological advantages beyond a basic diet. This systematic review aims to explain their significance in metabolic, behavioral, and musculoskeletal health, focusing on their therapeutic benefits, molecular mechanisms, and bioactivities. This systematic review analyzed clinical trials from PubMed and Scopus databases in the time range of 2019 to 2024, following the Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRISMA) standards, that investigated the role of peptides in human nutrition. Eight randomized clinical trials (RCTs) met the predefined metabolic, behavioral, and musculoskeletal health inclusion criteria. Peptides are derived from various sources, including milk, fish, and plants, and show various bioactive characteristics such as anti-inflammatory effect, improved muscle protein synthesis, and immune modulation. Some important findings emphasize their potential to govern metabolic processes, defend against chronic diseases, and enhance gut health. For instance, glucagon-like peptide (GLP-1) controls taste perception and appetite stimulation, and collagen peptides strengthen the musculoskeletal system. Peptides display intriguing potential as nutrients for addressing global health challenges, including behavioral responses, aging, and metabolic syndrome. Future investigations would focus on bioavailability, optimizing dosage, and demographic-specific treatments. Full article

Aging leads to a decline in skin function due to intrinsic factors (genetics, hormones) and extrinsic factors (sun exposure, pollutants). Type I collagen plays a vital role in maintaining skin integrity and elasticity. As aging progresses, collagen synthesis diminishes, resulting in weakened skin structure and wrinkle formation. This systematic review explores the role of type I collagen in skin aging by summarizing key clinical findings. A systematic search was conducted using PubMed and ScienceDirect as the primary databases, including studies published between 2014 and 2025 that addressed type I collagen and skin aging. Eleven clinical studies were selected following PRISMA guidelines. The results consistently show the decline of type I collagen as a central contributor to dermal thinning, loss of elasticity, and the appearance of wrinkles and sagging. Clinical trials demonstrate that collagen supplementation, particularly from hydrolyzed fish cartilage and low-molecular-weight peptides, enhances collagen production, improves skin hydration and texture, and reduces signs of photoaging. Overall, the evidence emphasizes the critical role of type I collagen in skin aging and suggests that targeted collagen supplementation may serve as an effective strategy to maintain skin structure and combat visible signs of aging. Full article

The marine environment, covering over 70% of the Earth’s surface, serves as a reservoir of bioactive molecules, including peptides and proteins. Due to the unique and often extreme marine conditions, these molecules exhibit distinctive structural features and diverse functional properties, making them promising candidates for therapeutic applications. Marine-derived bioactive peptides, typically consisting of 3 to 40 amino acid residues—though most commonly, 2 to 20—are obtained from parent proteins through chemical or enzymatic hydrolysis, microbial fermentation, or gastrointestinal digestion. Like peptides, protein hydrolysates from collagen, a dominant protein of such materials, play an important role. Peptide bioactivities include antioxidant, antihypertensive, antidiabetic, antimicrobial, anti-inflammatory, anticoagulant, and anti-cancer effects as well as immunoregulatory and wound-healing activities. These peptides exert their effects through mechanisms such as enzyme inhibition, receptor modulation, and free radical scavenging, among others. Fish, algae, mollusks, crustaceans, microbes, invertebrates, and marine by-products such as skin, bones, and viscera are some of the key marine sources of bioactive proteins and peptides. The advancements in the extraction and purification processes, e.g., enzymatic hydrolysis, ultrafiltration, ion-exchange chromatography, high-performance liquid chromatography (HPLC), and molecular docking, facilitate easy identification and purification of such bioactive peptides in greater purity and activity. Despite their colossal potential, their production, scale-up, stability, and bioavailability are yet to be enhanced for industrial applications. Additional work needs to be carried out for optimal extraction processes, to unravel the mechanisms of action, and to discover novel marine sources. This review emphasizes the enormous scope of marine-derived peptides and proteins in the pharmaceutical, nutraceutical, cosmeceutical, and functional food industries, emphasizing their role in health promotion and risk reduction of chronic diseases. Full article

Gelatin from deer has garnered attention as a high-value health-promoting resource given its history of usage as a traditional Chinese medicine and recent studies demonstrating its biological activities. Mass spectrometry-based methods have increasingly been employed for species identification in collagen-based materials, effectively addressing challenges in quality control and authenticity verification. This study aims to identify characteristic marker peptides in gelatins from sika deer (Cervus nippon) to support their effective use as a health-promoting resource. Gelatin samples were enzymatically digested, and the resulting peptide mixtures were analyzed using ultra-high-performance liquid chromatography coupled with quadrupole Q-Exactive-Orbitrap mass spectrometry (UHPLC-Q-Exactive-Orbitrap MS). Marker peptide candidates were selected based on their high detection intensity and a literature review. Among the 28 selected marker peptide candidates, four peptides (P11, R2, R3, and R4) were defined as characteristic of sika deer gelatin. Comparative analyses with gelatins derived from donkey hide, bovine, porcine, and fish samples further confirmed the specificity of these peptides. These findings establish a robust analytical method for verifying the authenticity of sika deer gelatin, contributing to its safe and effective use as a health-promoting resource. Full article

Marine-derived proteins, rich in amino acids and bioactivity, serve as a natural and safe alternative to chemical haircare products. This study selected three highly bioactive fish-derived protein peptides and determined their optimal repair ratio using FTIR structural analysis and response surface methodology (RSM). A collagen peptide-based composite human hair repair emulsion (CHFRE) was formulated, and its repair efficacy on damaged hair (DH) was evaluated using scanning electron microscopy (SEM), Fourier transform infrared spectroscopy (FTIR), differential scanning calorimetry (DSC), and amino acid analysis. Following CHFRE treatment, the physical and chemical properties of damaged hair improved significantly. SEM analysis revealed enhanced hair luster, aligned cuticle scales, and a denser cortex. FTIR and DSC analyses showed a 5.94% increase in α-conformation content and a 28.44% rise in relative helical content (RHC), indicating enhanced protein stability and a conformation closer to that of normal hair. Additionally, the 14.63% increase in S=O transmittance suggested reduced oxidative damage. Amino acid analysis and hydrophobic amino acids, with specific increments of 16.77 g/100 g and 2.47 g/100 g, respectively, enhance hair affinity and keratin stability. This bio-based repair material effectively restores damaged hair structure, strengthens resistance to chemical damage, and ensures sustainability, safety, and biocompatibility, providing a promising approach for the development of natural hair repair products. Full article

The circular economy of animal by-products rich in collagen focuses on converting collagen into peptides with a defined molecular weight. Collagen hydrolysates prepared by biotechnological methods from chicken gizzards, deer tendons, and Cyprinus carpio skeletons can be an alternative source of collagen for cosmetic products that traditionally use bovine or porcine collagen hydrolysates. Collagen hydrolysates were characterized by antioxidant activity, surface tension, solution contact angle, and other parameters (dry weight, ash content, and solution clarity). Furthermore, the vibrational characterization of functional groups and their molecular weight was performed using the GPC-RID method. Subsequently, emulsion and gel cosmetic matrices were prepared with 0.5% and 1.5% collagen hydrolysates. Microbiological stability, organoleptic properties, and viscosity were investigated. Verification of the biophysical parameters of the topical formulations was performed in vivo on a group of volunteers by measuring skin hydration and pH and determining trans-epidermal water loss. Fish collagen hydrolysate was the most suitable for cosmetic applications in the parameters investigated. Moreover, it also effectively reduces wrinkles in the periorbital region when used in a gel matrix. Full article

The high biocompatibility and the key role of collagen in bone extracellular matrix make it useful for tissue engineering. However, the high demand, costs, and challenges of extracting good-quality collagen have led to the use of collagen derivatives and search for non-human alternatives. This study investigates fish and bovine collagen peptides (Coll_f and Coll_b, respectively) as sustainable sources for 3D-printed bone scaffolds by developing and characterizing peptide-incorporated alginate/hydroxyapatite-based bioinks. The chemical analysis revealed structural similarities between the peptides, while rheological tests showed a slightly higher viscosity of Coll_f-based inks, which improved shape fidelity during the printing process. Upon oscillating rheological tests, both the Coll_f and Coll_b-based ink formulations demonstrated a solid-like behavior at frequencies higher than 0.4 Hz, which is crucial for maintaining the printed structure integrity during extrusion. Although Coll_b-based inks exhibited better pore printability, Coll_f-based inks achieved superior resolution and geometry retention. Macro-porous structures printed from both inks showed good accuracy, with minimal shrinkage attributed to hydroxyapatite. Both the produced inks had a high gel fraction and swelling behavior, with Coll_b-based outperforming Coll_f-based inks. Finally, both ink formulations resulted to be cytocompatibile with human dermal fibroblasts. These findings position Coll_f- and Coll_b-based inks as promising alternatives for bone tissue scaffolds, offering a sustainable balance between performance and structural stability in 3D printing applications. Full article

Vitamin C is an organic compound biosynthesized in plants and most vertebrates. Since its discovery, the benefits of vitamin C use in the cure and prevention of various pathologies have been frequently reported, including its anti-oxidant, anti-inflammatory, anticoagulant, and immune modulatory properties. Vitamin C plays an important role in collagen synthesis and subsequent scurvy prevention. It is also required in vivo as a cofactor for enzymes involved in carnitine and catecholamine norepinephrine biosynthesis, peptide amidation, and tyrosine catabolism. Moreover, as an enzymatic cofactor, vitamin C is involved in processes of gene transcription and epigenetic regulation. The absence of the synthesis of L-gulono-1,4-lactone oxidase, a key enzyme in the pathway of vitamin C synthesis, is an inborn metabolism error in some fishes and several bird and mammalian species, including humans and non-human primates; it is caused by various changes in the structure of the original GULO gene, making these affected species dependent on external sources of vitamin C. The evolutionary cause of GULO gene pseudogenization remains controversial, as either dietary supplementation or neutral selection is evoked. An evolutionary improvement in the control of redox homeostasis was also considered, as potentially toxic H₂O₂ is generated as a byproduct in the vitamin C biosynthesis pathway. The inactivation of the GULO gene and the subsequent reliance on dietary vitamin C may have broader implications for aging and age-related diseases, as one of the most important actions of vitamin C is as an anti-oxidant. Therefore, an important aim for medical professionals regarding human and animal health should be establishing vitamin C homeostasis in species that are unable to synthesize it themselves, preventing pathologies such as cardiovascular diseases, cognitive decline, and even cancer. Full article

Wound healing incurs various challenges, making it an important topic in medicine. Short-chain peptides from fish protein hydrolysates possess wound healing properties that may represent a solution. In this study, perch hydrolysates were produced from perch side steams using a designed commercial complex enzyme via a proprietary pressure extraction technique. The average molecular weight of the perch peptides was 1289 kDa, and 62.60% of the peptides had a low molecular weight (≤1 kDa). Similarly to the beneficial amino acid sequence FPSIVGRP, FPSLVRGP accounted for 6.21% abundance may have a potential antihypertensive effect. The concentrations of collagen composition and branched-chain amino acids were 1183 and 1122 mg/100 g, respectively. In a fibroblast model, active perch peptides accelerated wound healing mainly by increasing the secretion of procollagen I, fibronectin, and hyaluronan. In an SD rat model established to mimic human wounds, orally administered perch hydrolysates with a molecular weight below 2.3 kDa accelerated wound healing, which mainly resulted from collagen-forming amino acids, branched-chain amino acids, and matrikine. Collectively, the residue of perch extract can be upcycled via a hydrolysis technique to produce not only bioactive sequences but also short-chain peptides. Considering the therapeutic potential to promote wound healing, such by-products are of great value and may be developed as dietary nutraceuticals. Full article

In this investigation, collagen was successfully extracted from the skin and fins of the orange-spotted grouper, Epinephelus coioides, with recovery rates of 4.45% and 23.65% (dry weight basis), respectively. UV–Vis spectrophotometric analysis demonstrated distinct absorbance peaks at 222 nm and 217 nm for collagen isolated from the skin and fins, correspondingly. Both collagen sources were confirmed to be type I, characterized by the presence of two α-chains (α1 and α2), with glycine as the predominant amino acid, an absence of tryptophan, and a notable content of proline and hydroxyproline. The enzymatic hydrolysis of fin-derived collagen using pepsin yielded low-molecular-weight peptides (PHC), which were subsequently incorporated into the diet of 1.5-year-old zebrafish, either alone or in combination with glucosamine (GC), to assess their biological effects. After eight weeks of dietary supplementation, zebrafish fed PHC or the combined PHC + GC diets exhibited a significant upregulation of sox9a (jef) expression in spinal tissues, accompanied by a marked downregulation of runx2. Although the differences in swimming performance among the groups were not statistically significant, zebrafish that received PHC or the combined supplements demonstrated enhanced endurance compared to the control group. These results suggest that collagen sourced from grouper may have advantageous effects in supporting cartilage health in aged zebrafish. Furthermore, utilizing fish by-products for collagen extraction enhances resource efficiency and aligns with circular economy principles. Full article

Background: Anabolic resistance accelerates muscle loss in aging and obesity, thus predisposing to sarcopenic obesity. Methods: In this retrospective analysis of a randomized clinical trial, we examined baseline predictors of the adaptive response to three months of home-based resistance exercise, daily physical activity, and protein-based, multi-ingredient supplementation (MIS) in a cohort of free-living, older males (n = 32). Results: Multiple linear regression analyses revealed that obesity and a Global Risk Index for metabolic syndrome (MetS) were the strongest predictors of Δ% gains in lean mass (TLM and ASM), LM/body fat ratios (TLM/%BF, ASM/FM, and ASM/%BF), and allometric LM (ASMI, TLM/BW, TLM/BMI, ASM/BW), with moderately strong, negative correlations to the adaptive response to polytherapy r = −0.36 to −0.68 (p < 0.05). Kidney function, PA level, and chronological age were only weakly associated with treatment outcomes (p > 0.05). Next, we performed a subgroup analysis in overweight/obese participants with at least one other MetS risk factor and examined their adaptive response to polytherapy with two types of protein-based MIS (PLA; collagen peptides and safflower oil, n = 8, M5; whey/casein, creatine, calcium, vitamin D₃, and fish oil, n = 12). The M5 group showed greater improvements in LM (ASM; +2% vs. −0.8%), LM/body fat ratios (ASM/FM; +3.8% vs. −5.1%), allometric LM (ASM/BMI; +1.2% vs. −2.5%), strength (leg press; +17% vs. −1.4%), and performance (4-Step-Stair-Climb time; −10.5% vs. +1.1%) vs. the PLA group (p < 0.05). Bone turnover markers, indicative of bone accretion, were increased pre-to-post intervention in the M5 group only (P1NP; p = 0.036, P1NP/CTX ratio; p = 0.088). The overall anabolic response, as indicated by ranking low-to-high responders for Δ% LM (p = 0.0079), strength (p = 0.097), and performance (p = 0.19), was therefore significantly higher in the M5 vs. PLA group (p = 0.013). Conclusions: Our findings confirm that obesity/MetS is a key driver of anabolic resistance in old age and that a high-quality, whey/casein-based MIS is more effective than a collagen-based alternative for maintaining musculoskeletal health in individuals at risk for sarcopenic obesity, even when total daily protein intake exceeds current treatment guidelines. Full article

Background. Urinary collagen peptides, the breakdown products of endogenous collagen, have been used as biomarkers for various diseases. These non-invasive biomarkers are easily measured via mass spectrometry, aiding in diagnostics and therapy effectiveness. Objectives. The objective of this study was to investigate the effects of consuming collagen-containing meat on collagen peptide composition in human blood and urine. Methods. Ten collagen peptides in 24 h urine were quantified. Results. Prolyl-hydroxyproline (Pro-Hyp) was the most abundant peptide. Except for hydroxyprolyl-glycine (Hyp-Gly), levels of other minor collagen peptides showed high correlation coefficients with Pro-Hyp (r = 0.42 vs. r > 0.8). Notably, 24 h urinary Hyp-Gly showed a correlation coefficient of r = 0.72 with meat consumption, significantly higher than the coefficient for Pro-Hyp (r = 0.37). Additionally, the levels of Pro-Hyp and Hyp-Gly in the blood of seven young women participants increased similarly after consuming fish meat, while before ingestion, only negligible amounts of Hyp-Gly were present. To examine which peptides are generated by the degradation of endogenous collagen, mouse skin was cultured. The amount of Pro-Hyp released from the skin was approximately 1000-fold higher than that of Hyp-Gly. Following consumption of collagen-containing meat, both Pro-Hyp and Hyp-Gly are released in blood and excreted into urine, although Pro-Hyp is primarily generated from endogenous collagen even under physiological conditions. Conclusions. Therefore, in 24 h urine samples, the non-negligible fraction of Pro-Hyp is contributed by endogenous collagen, making 24 h urine Hyp-Gly level a potential biomarker for evaluating meat consumption on the day. Full article

Background/Objectives: Marine collagen peptides (MCPs) and glycosaminoglycans (GAGs) have been described as potential wound-healing (WH) agents. Fish cartilage hydrolysate (FCH) is a natural active food ingredient obtained from enzymatic hydrolysis which combines MCPs and GAGs. Recently, the clinical benefits of FCH supplementation for the skin, as well as its mode of action, have been demonstrated. Some of the highlighted mechanisms are common to the WH process. The aim of the study is therefore to investigate the influence of FCH supplementation on the skin healing processes and the underlying mechanisms. Methods: To this end, an ex vivo clinical approach, which takes into account the clinical digestive course of nutrients, coupled with primary cell culture on human dermal fibroblasts (HDFs) and ultra-deep proteomic analysis, was performed. The effects of human serum enriched in circulating metabolites resulting from FCH ingestion (FCH-enriched serum) were assessed on HDF WH via an in vitro scratch wound assay and on the HDF proteome via diaPASEF (Data Independent Acquisition—Parallel Accumulation Serial Fragmentation) proteomic analysis. Results: Results showed that FCH-enriched human serum accelerated wound closure. In support, proteins with anti-inflammatory and immunomodulatory properties and proteins prone to promote hydration and ECM stability showed increased expression in HDFs after exposure to FCH-enriched serum. Conclusions: Taken together, these data provide valuable new insights into the mechanisms that may contribute to FCH’s beneficial impact on human skin functionality by supporting WH. Further studies are needed to reinforce these preliminary data and investigate the anti-inflammatory and immunomodulatory properties of FCH. Full article

Collagen peptides and marine collagen are enormous resources currently utilized. This review aims to examine the scientific literature to determine which collagen peptides derived from marine sources and which natural active antioxidants from marine collagen have significant biological effects as health-promoting nutraceuticals. Marine collagen is extracted from both vertebrate and invertebrate marine creatures. For vertebrates, this includes fish skin, bones, scales, fins, and cartilage. For invertebrates, it includes mollusks, echinoderms, crustaceans, and poriferans. The method used involved data analysis to organize information for isolating and identifying marine biocompounds with antioxidant properties. Specifically, amino acids with antioxidant properties were identified, enabling the use of hydrolysates and collagen peptides as natural antioxidant nutraceuticals. The methods of extraction of hydrolyzed collagen and collagen peptides by different treatments are systematized. The structural characteristics of collagen, collagen peptides, and amino acids in fish skin and by-products, as well as in invertebrate organisms (jellyfish, mollusks, and crustaceans), are described. The antioxidant properties of different methods of collagen hydrolysates and collagen peptides are systematized, and the results are comparatively analyzed. Their use as natural antioxidant nutraceuticals expands the range of possibilities for the exploitation of natural resources that have not been widely used until now. Full article