Search Results (26)

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

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

The valorization of aquaculture/fishery processing by-products, as well as unavoidable/unwanted catches and discards in Greece, is currently an underutilized activity despite the fact that there are several best practices in Northern Europe and overseas. One of the main challenges is to determine whether the available quantities for processing are sufficient to warrant the valorization of discards and fish side streams. This is the first attempt to systematically record and analyze the available quantities of fish by-products and discards in Greece spatially and temporally in an effort to create a national exploitation Master Plan for the valorization of this unavoidable and unwanted biomass. A thorough survey conducted within the VIOAXIOPIO project unveiled a substantial biomass of around 19,000 tonnes annually that could be harnessed for valorization. Furthermore, the production of various High-Added-Value Biomolecules (HAVBs) was investigated and experimental trials were conducted to assess the potential yields, with the collected data used to formulate four valorization scenarios. Full article

The enzymatic extraction of proteins from fish biomasses is being widely investigated. However, little or almost no research has paid attention to the exploitation of unsorted fishery biomasses. This work is part of a larger study, Part I of which has already been published, and focuses on an extensive characterization of two collagenous samples, namely gelatin (G) and hydrolyzed gelatin peptides (HGPs), extracted from a dehydrated fish biomass coming from unsorted canned yellowfin tuna side streams. The results indicate crude protein fractions of 90–93%, pH values between 3 and 5, white–yellow colors, collagen-like FTIR spectra, and 17% in terms of total amino acid content. Viscosity and the study of dynamic viscous–elastic behavior were analyzed. Thermo-gravimetric analysis was performed to assess the residual ashes. Both samples were investigated to determine their molecular weight distribution via size-exclusion chromatography, with a higher total average molecular weight for G compared to HGPs, with values of 17,265.5 Da and 2637.5 Da, respectively. G demonstrated technological properties similar to analogous marine gelatins. HGPs demonstrated antioxidant activity as per FRAP assay. All the results open up new perspectives for the potential use of these substances in biodegradable packaging, dietary supplements, and skin care cosmetics. Full article

Considering the global increase in fish consumption, the growing side-streams coming from the fish supply chain (e.g., skin, fins, tail, heads…), also including undersized or “unwanted catches”, have been recently proposed as source of high-value bioactive compounds (e.g., peptides and fatty acids). In this case study, hydrolyzed collagen peptides (HCPs) were extracted from different parts of Mugil cephalus L. using environmentally friendly techniques such as ultrasounds and enzymatic treatments. Both a mixed biomass derived from the skin, fins, and tail, and a whole fish, were considered as starting biomass, simulating the unsorted processing side-streams and an undersized/unwanted catch, respectively. The extracted HCPs were purified in fractions (<3 KDa and >3 KDa) whose yields (about 5% and 0.04–0.3%, respectively) demonstrated the efficiency of the hydrolysis process. The extraction protocol proposed allowed us to also isolate the intermediate products, namely the lipids (about 8–10%) and the non-collagenous proteins (NCs, 16–23%), whose exploitation could be considered. Each sample was characterized using Sircol, UltraViolet-Spectra, and hydroxyproline assay, and the viability of their collagen fractions was tested on human endothelial cells. Significant effects were obtained at a fraction of <3 KDa, in particular at a concentration of 0.13 µg/mL. The T-scratch test was also performed, with positive results in all fractions tested. Full article

Hydrolyzed collagen, glycogen, and hyaluronic acid, obtained through the biotechnological valorization of underutilized marine bioresources, fulfill cosmetic industry requirements for sustainable products produced under circular economy principles. Hydrolyzed collagen was obtained by hydrolyzing blue shark collagen with papain and ultrafiltration. Glycogen was isolated from industrial mussel cooking wastewaters through ultrafiltration, precipitation, and selective polysaccharide separation. Hyaluronic acid was produced by fermentation, purification, and depolymerization. The main objective was to test the feasibility of including these three biomolecules in a cosmetic formulation as bioactive compounds. For this, the in vitro irritant potential of the three ingredients and also that of the cosmetic formulation was assayed according to the Reconstituted Human Epithelium Test method OECD 439. Moreover, an in vitro assessment of the effect of hydrolyzed collagen and hyaluronic acid combinations on mRNA expression and collagen type I synthesis was evaluated in adult human fibroblasts. This study establishes, for the first time, the potential use of particular hydrolyzed collagen and hyaluronic acid combinations as stimulators of collagen I synthesis in fibroblast cultures. Besides, it provide safety information regarding potential use of those biomolecules in the formulation of a cosmetic preparation positively concluding that both, ingredients and cosmetic preparation, resulted not irritant for skin following an international validated reference method. Full article

Seabass (Lates calcarifer) is one of the top farmed and raised fish in Taiwan, and fish scales are the main by-product after processing. Fish scales contain high amounts of collagen, which can chelate with minerals and enhance mineral absorption in the human body. Hence, fish scales from seabass were enzymatically hydrolyzed to obtain seabass scale collagen peptide (SBSCP). Calcium, the most consumed mineral supplement, was chelated with SBSCP to form SBSCP-Ca. The optimal conditions for chelation were a peptide/calcium ratio: 1:1 (w/w), pH 5.0, and 50 °C for 20 min. The conjugated sites were carboxyl and amino groups based on Fourier transform infrared (FTIR) spectroscopy. Scanning electronic microscope/energy-dispersive X-ray spectroscopy (SEM/EDS) evidently showed the alternation of SBSCP’s molecular structure after chelation and increased concentrations of metal ions. SBSCP-Ca was stable up to 90 °C and from pH 2.0 to 5.0. The retention rate was 70%, as determined after in vitro digestion. The extracts of blackcurrant or berry-grape seeds were added to neutralize the fishy odor and provide antioxidant ability for commercialization. This is the first complete study of the characteristics of SBSCP-Ca as well as their commercialization. Full article

A large amount of fish side streams are produced each year, promoting huge economic and environmental problems. In order to address this issue, a potential alternative is to isolate the high-added-value compounds with beneficial properties on human health. The objectives of this study were to determine the effect of hydrolyzed fish protein and collagen samples on cell proliferation, as well as to determine the specific influence of minerals and metals on this effect and whether dietary antioxidants can enhance cell proliferation. The results of hydrolyzed fish protein and collagen samples showed negative effects on Caco-2 cell proliferation at the highest concentrations tested. Moreover, the pre-treatment of these hydrolyzates with vitamin C and E, quercetin and resveratrol increased the proliferation of bioaccessible fractions of hydrolyzated fish protein and collagen samples compared to the bioaccessible fractions without pre-treatment. The highest mineral concentrations were found for P, Ca and Mg. The metals found in the pure hydrolyzates were As, Cd, Hg and Pb; however, they appeared at almost undetectable levels in bioavailable fractions. It can be concluded that the consumption of hydrolyzates of fish by-products is an interesting strategy for complying with EFSA recommendations regarding fish consumption while at the same time reducing fish waste. Full article

Fish by-products are rich in collagen. Hydrolyzed collagen derived from fish by-products was used to replace fish meal to evaluate the effects on muscle quality and glycolipid metabolism of juvenile triploid crucian carp. A total of 240 juvenile fish with body weight of 10.01 ± 0.02 g were divided into four groups and fed four diets for 66 days: fish meal (FM) replaced with hydrolyzed collagen (HC) in 0% (Control), 2% (2% HC), 4% (4% HC), and 6% (6% HC), respectively. The results were as follows: The increased proportion of fish meal replaced with hydrolyzed collagen linearly and quadratically decreased the specific growth rate (SGR) of triploid crucian carp (p < 0.05). Compared with the control group, the SGR and intestinal α-amylase, trypsin and lipase activities in the 4% and 6% HC groups significantly decreased (p < 0.05), while there was no significant difference between the control and 2% HC groups (p > 0.05). Total umami amino acids content, chewiness and myofiber density of muscle in the 4% and 6% HC groups, as well as the essential fatty acids content in all HC groups increased significantly (p < 0.05). All HC groups significantly increased the serum glutathione peroxidase (GSH-Px) activity and decreased the serum malondialdehyde (MDA) content (p < 0.05). When the replacement amount reached 4%, the serum glucose and liver glycogen content, the liver and serum triglyceride (TG) content, and serum total cholesterol (T-CHO) content were significantly reduced (p < 0.05). In addition, the expression levels of insulin-like growth factor-1 (IGF-1) of the liver in all HC groups and lipolysis-related genes (lipoprotein lipase (LPL), carnitine O-palmitoyltransferase 1 (CPT 1) and hydroxyacyl-coenzyme A dehydrogenase (HADH)) of the liver in the 6% of HC group increased significantly (p < 0.05), and the expression levels of lipogenesis-related genes (fatty acid synthase (FAS) and sterol regulatory element-binding protein 1 (SREBP 1)) of the liver in the 4% HC and 6% HC groups decreased significantly (p < 0.05). In conclusion, the replacement of 2% fish meal with hydrolyzed collagen had no negative effects on the growth of triploid crucian carp, while the replacement of 4% fish meal with hydrolyzed collagen decreased SGR, but improved the muscle quality and decreased glycolipid levels. The maximum proportion of hydrolyzed collagen replacing fish meal should not exceed 4%. Full article

To stop overfishing and meet the protein needs of a growing population, more information is needed on how to use marine by-catches, by-products, and undervalued fish species for human consumption. Turning them into protein powder is a sustainable and marketable way to add value. However, more knowledge of the chemical and sensory properties of commercial fish proteins is needed to identify the challenges in developing fish derivatives. This study aimed to characterize the sensory and chemical properties of commercial fish proteins to compare their suitability for human consumption. Proximate composition, protein, polypeptide and lipid profiles, lipid oxidation, and functional properties were analyzed. The sensory profile was compiled using generic descriptive analysis, and odor-active compounds were identified with gas-chromatography–mass spectrometry-olfactometry (GC-MS/O). Results indicated significant differences in chemical and sensory properties between processing methods but not between fish species. However, the raw material had some influence in the proteins’ proximate composition. Bitterness and fishiness were the main perceived off-flavors. All samples, apart from hydrolyzed collagen, had intense flavor and odor. Differences in odor-active compounds supported the sensory evaluation results. The chemical properties revealed that the lipid oxidation, peptide profile, and raw material degradation are likely affecting the sensory properties of commercial fish proteins. Limiting lipid oxidation during processing is crucial for the development of mild-tasting and -smelling products for human consumption. Full article

Fish collagen is a good source of protein and essential amino acids. It has a wide range of applications in food manufacturing, pharmaceutics, cosmetics, etc. By-products obtained from fish processing industries are currently used as alternative sources for the production of collagen and gelatin. Hydrolyzed collagen derived from fish skin has properties that are beneficial in cosmetic products. The aim of this study was to: (1) formulate a cosmetic product containing hydrolyzed fish collagen obtained from a by-product of fish processing industries, and other effective ingredients such as vitamin C, vitamin E and vitamin B3, (2) evaluate the physicochemical properties and stability of the product, and (3) conduct a facial skin evaluation test wherein volunteers use the product and have their facial skin analyzed. The formulated serum was translucent with low turbidity and had a pH of 7.7, and a viscosity of 1333 cps. The stability of the formulation was good, without any significant change in appearance, pH and viscosity as tested by freeze–thaw cycle testing, and after storage at room temperature for a period of 6 months. Furthermore, the results from the Visia skin analysis instrument revealed that the product was able to enhance facial skin moisture, reduce skin pores and wrinkles, and brighten the skin significantly when regularly used for at least 2 weeks. In conclusion, it was observed that hydrolyzed fish collagen obtained from a by-product of fish processing industries could be a sustainable and suitable material utilized in the production of safe and useful cosmeceutical products. Full article

Skin injury causes fibroblast dysfunction and lowers collagen production. Safe, functional ingredients such as vitamin C (Vit C) and fish hydrolyzed collagen (HC) have been used to alleviate this problem. Defatted HC from salmon (Oncorhynchus nerka) skin could be a potential functional ingredient with skin nourishment activity. This study aimed to investigate the combined effects of HC and Vit C on the proliferation and migration of human dermal fibroblast (HDF). Molecular weight ranging from 102 Da to 10,175 Da and high imino acid content were found in HC. HC (0–800 µg/mL) or vitamin C (Vit C) (0.01–100 µg/mL) was applied for HDF treatment. Higher cell proliferation was found by adding HC at 50 µg/mL or Vit C at 0.01 µg/mL compared to the control and those treated with both compounds at other levels (p < 0.05). Cells treated with HC (50 µg/mL) combined with Vit C (0.01 µg/mL) (HC+Vit C) showed higher proliferation, migration, and lamellipodia formation of HDF cells than those treated with HC or Vit C alone. Moreover, all the samples tested could stimulate the proliferation and migration of HDF cells via FAK/Akt and ERK/p38 MAPK signaling pathways. Thus, HC combined with Vit C could be a promising functional ingredient for skin nourishment and would healing. Full article

The skin of mackerel scad fish (Decapterus macarellus) is a new source for pepsin-soluble collagen and its hydrolysate, both of which have never been explored. This study aims to characterize and determine the in vitro antioxidant, antiglycation, and antityrosinase activity of pepsin-soluble collagen (PSC) and hydrolyzed collagen (HC) from mackerel scad skin. PSC was extracted using 0.5 M acetic acid containing 0.1% pepsin for 48 h at 4 °C. The obtained PSC was then hydrolyzed with collagenase type II (6250 U/g) to produce HC. The PSC yield obtained was 6.39 ± 0.97%, with a pH of 6.76 ± 0.18, while the HC yield was 96% from PSC. SDS-PAGE and Fourier Transform Infrared (FTIR) analysis showed the typical features of type I collagen. HC demonstrated high solubility (66.75–100%) throughout the entire pH range (1–10). The PSC and HC from mackerel scad skin showed antioxidant activity against 2,2-diphenyl-1-picrylhydrazyl (DPPH), with IC50 values of 148.55 ± 3.14 ppm and 34.966 ± 0.518 ppm, respectively. In the antiglycation test, PSC had an IC50 value of 239.29 ± 15.67 ppm, while HC had an IC50 of 68.43 ± 0.44 ppm. PSC also exhibited antityrosinase activity, with IC50 values of 234.66 ± 0.185 ppm (on the L-DOPA substrate), while HC had an IC50 value of 79.35 ± 0.5 ppm. Taken together, these results suggest that the skin of mackerel scad fish has potential antiaging properties and can be further developed for pharmaceutical and cosmetic purposes. Full article

Type I collagen is the main component of the extracellular matrix that acts as the physical and biochemical support of tissues. Thanks to its characteristics, collagen is widely employed as a biomaterial for implantable device fabrication and as antiaging food supplementation. Because of the BSE transmission in the 1990s, aquatic animals have become a more suitable extraction source than warm-blooded animals. Moreover, as recently demonstrated, a supplementing diet with fish collagen can increase the body’s collagen biosynthesis. In this context, Tilapia feeding was supplemented with hydrolyzed collagen in order to enhance the yield of extracted collagen. Tilapia skin was investigated with wide and small angle scattering techniques, analyzing the collagen structure from the submolecular to the nanoscale and correlated with Differential Scanning Calorimetry (DSC) measurements. Our studies demonstrated that the supplementation appears to have an effect at the nanoscale in which fibrils appear more randomly oriented than in fish fed with no supplemented feed. Conversely, no effect of a collagen-rich diet was observed at the submolecular scale. Full article

Lipid oxidation has a negative impact on application and stability of hydrolyzed collagen (HC) powder from fatty fish skin. This study aimed to produce fat-free HC powder from salmon skin via optimization of one-step hydrolysis using mixed proteases (papain and Alcalase) at different levels. Fat removal processes using disk stack centrifugal separator (DSCS) for various cycles and subsequent defatting of HC powder using isopropanol for different cycles were also investigated. One-step hydrolysis by mixed proteases (3% papain and 4% Alcalase) at pH 8 and 60 °C for 240 min provided HC with highest degree of hydrolysis. HC powder having fat removal with DSCS for 9 cycles showed the decreased fat content. HC powder subsequently defatted with isopropanol for 2 cycles (HC-C9/ISP2) had no fat content with lowest fishy odor intensity, peroxide value, and thiobarbituric acid reactive substances than those without defatting and with 1-cycle defatting. HC-C9/ISP2 had high L*-value (84.52) and high protein (94.72%). It contained peptides having molecular weight less than 3 kDa. Glycine and imino acids were dominant amino acid. HC-C9/ISP2 had Na, Ca, P, and lowered odorous constituents. Combined processes including hydrolysis and defatting could therefore render HC powder free of fat and negligible fishy odor. Full article