• Journal of the Korean Applied Science and Technology
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• v.26 no.4
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• pp.457-466
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• 2009

This study is manufacturing method and analysis of feasibility about collagen peptide from fish scale. This is processed by enzyme hydrolysis, isolating and refining etc. The results of analysis of nutritional composition showed protein content of collagen peptide. In the analysis of constitutive amino acids, the ratio of contents of hydroxyproline and glycine, the characteristics of collagen peptides appeared similar and the contents of glutamic acid and aspartic acid which are involved in protein metabolism. As a result of measurement of total polyphenol content and total flavonoid, it showed that collagen peptide had more contents generally, and the effect of bioactivity of pig-skin collagen peptide appeared higher although different kinds of scale collagen peptide showed a little DPPH radical scavenging ability, total antioxidant capacity by ABTS, ACE inhibitory.

• Korean Journal of Food Science and Technology
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• v.53 no.6
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• pp.695-700
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• 2021

The purpose of this study was to prepare low-molecular weight collagen using a commercial proteolytic enzyme (Protamex) from collagen extracted from feet of Korean native chicken and to investigate the quality characteristics of this collagen. The collagen content of Korean native chicken feet was 13.9 g/100 g, which was higher than the 6.21 g/100 g of general broilers. It was found that the content of low molecular weight collagen increased as the concentration of proteolytic enzymes and reaction time increased. In particular, reaction with 1% Protamex for 7 h resulted in 55.6% of low molecular weight (1,000-5,000 Da) collagen content, and the average molecular weight was 5,390 Da. Regarding the texture of the enzyme-treated collagen, the collagen with high molecular weight peptides decomposed into low molecular weight peptides, and the gel type could not be formed, whereas the sol type was maintained.

• Journal of Life Science
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• v.25 no.3
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• pp.269-275
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• 2015

Collagen peptides, which are found at high concentrations in the human body, are present in animal bones and the skin of marine organisms, namely, fish scales. Collagen is the most abundant structural protein of various connective tissues in animals. Furthermore, it is widely used in biomedical material, pharmaceutical, cosmetic, food, and leather industries. Peptides extracted from scales of various fish protect against ultraviolet B (UVB)-induced skin damage and photo-aging. However, the protective effects of collagen peptides derived from the scales of Branchiostegus japonicus against UVB exposure are unclear. This study investigated the effects of peptides larger than 1 kDa (high-molecular weight peptides [HMP]) and smaller than 1 kDa (low-molecular weight peptides [LMP]), derived from extracts of B. japonicus scales, against UVB-induced skin damage and photo-aging. These peptides scavenged 1,1-diphenyl-2-picrylhydrazyl radicals in a dose-dependent manner. In UVB-exposed HaCaT human keratinocytes, LMP inhibited 8-isoprostane generation, a marker of cellular lipid peroxidation. The peptides also suppressed the UVB-induced increase in tyrosinase activity and melanin content in B16F10 mouse melanoma cells. In addition, the LMP and HMP treatment suppressed UVB-induced elastase and matrix metalloproteinase-1 activities in the HaCaT cells. These results indicate that peptides derived from B. japonicus scales have antioxidant, antiphoto-aging, and skin-whitening effects.

• Food Science of Animal Resources
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• v.35 no.2
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• pp.156-163
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• 2015

The effects of low molecular-weight collagen peptides derived from porcine skin were investigated on the physicochemical and sensorial properties of chocolate ice cream. Collagen peptides less than 1 kDa in weight were obtained by sub-critical water hydrolysis at a temperature of $300^{\circ}C$ and a pressure of 80 bar. Ice cream was then prepared with gelatin powder and porcine skin hydrolysate (PSH) stabilizers mixed at seven different ratios (for a total of 0.5 wt%). There was no significant difference in color between the resulting ice cream mixtures. The increase in apparent viscosity and shear thinning of the ice cream was more moderate with PSH added than with gelatin. Moreover, the samples containing more than 0.2 wt% PSH had enhanced melting resistance, while the mixture with 0.2 wt% PSH had the lowest storage modulus at $-20^{\circ}C$ and the second highest loss modulus at 10℃, indicating that this combination of hydrocolloids leads to relatively softer and creamier chocolate ice cream. Among the seven types of ice creams tested, the mixture with 0.2 wt% PSH and 0.3 wt% gelatin had the best physicochemical properties. However, in sensory evaluations, the samples containing PSH had lower chocolate flavor scores and higher off-flavor scores than the sample prepared with just 0.5 wt% gelatin due to the strong off-flavor of PSH.

• Journal of Microbiology and Biotechnology
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• v.32 no.11
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• pp.1382-1389
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• 2022

Asterias pectinifera, a species of starfish and cause of concern in the aquaculture industry, was recently identified as a source of non-toxic and highly water-soluble collagen peptides. In this study, we investigated the antioxidant and anti-photoaging functions of compounds formulated using collagen peptides from extracts of Asterias pectinifera and Halocynthia roretzi (AH). Our results showed that AH compounds have various skin protective functions, including antioxidant effects, determined by measuring the scavenging activity of 2,2-diphenyl-1-picrylhydrazyl radicals, as well as anti-melanogenic effects, determined by measuring tyrosinase inhibition activity. To determine whether ethosome-encapsulated AH compounds (E(AH)) exert ultraviolet (UV)-protective effects, human dermal fibroblasts or keratinocytes were incubated with E(AH) before and after exposure to UVA or UVB. E(AH) treatment led to inhibition of photoaging-induced secretion of matrix metalloproteinase-1 and interleukin-6 and -8, which are associated with inflammatory responses during UV irradiation. Finally, the antibacterial effects of AH and E(AH) were confirmed against both gram-negative and gram-positive bacteria. Our results indicate that E(AH) has the potential for use in the development of cosmetics with a range of skin protective functions.

• BMB Reports
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• v.53 no.10
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• pp.539-544
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• 2020

Skin aging appears to be the result of overlapping intrinsic (including genetic and hormonal factors) and extrinsic (external environment including chronic light exposure, chemicals, and toxins) processes. These factors cause decreases in the synthesis of collagen type I and elastin in fibroblasts and increases in the melanin in melanocytes. Collagen Type I is the most abundant type of collagen and is a major structural protein in human body tissues. In previous studies, many products containing collagen derived from land and marine animals as well as other sources have been used for a wide range of purposes in cosmetics and food. However, to our knowledge, the effects of human collagen-derived peptides on improvements in skin condition have not been investigated. Here we isolate and identify the domain of a human COL1A2-derived protein which promotes fibroblast cell proliferation and collagen type I synthesis. This human COL 1A2-derived peptide enhances wound healing and elastin production. Finally, the human collagen alpha-2 type I-derived peptide (SMM) ameliorates collagen type I synthesis, cell proliferation, cell migration, and elastin synthesis, supporting a significant anti-wrinkle effect. Collectively, these results demonstrate that human collagen alpha-2 type I-derived peptides is practically accessible in both cosmetics and food, with the goal of improving skin condition.

• Journal of Dairy Science and Biotechnology
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• v.31 no.2
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• pp.161-164
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• 2013

The prevalence rate of osteoporosis in older men and women has recently increased, and thus bone health is a major concern in Korea. This concern, along with increasing concern regarding youth height, has led to growth of the functional food industry for children, reaching approximately 200 billion won. It is necessary to develop safe and effective functional materials for bone growth and health. Foods are excellent sources of functional material as they are safe to use. It is well known that the phosphopeptide casein, which is derived from milk, is effective against osteoporosis by aiding in the absorption of calcium. In our study, collagen peptides derived from porcine skin were evaluated as a functional material for bone growth, as several peptides have been shown to aid in osteoblast formation.

• Preventive Nutrition and Food Science
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• v.18 no.2
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• pp.124-132
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• 2013

In this study, novel peptides (NIPP-1, NIPP-2) derived from Navicula incerta (microalgae) protein hydrolysate were explored for their inhibitory effects on collagen release in hepatic fibrosis with the investigation of its underlying mechanism of action. TGF-${\beta}1$ activated fibrosis in LX-2 cells was examined in the presence or absence of purified peptides NIPP-1 and NIPP-2. Besides the mechanisms of liver cell injury, protective effects of NIPP-1 and NIPP-2 were studied to show the protective mechanism against TGF-${\beta}1$ stimulated fibrogenesis. Our results showed that the core protein of NIPP-1 peptide prevented fibril formation of type I collagen, elevated the MMP level and inhibited TIMP production in a dose-dependent manner. The treatment of NIPP-1 and NIPP-2 on TGF-${\beta}1$ induced LX-2 cells alleviated hepatic fibrosis. Moreover, ${\alpha}$-SMA, TIMPs, collagen and PDGF in the NIPP-1 treated groups were significantly decreased. Therefore, it could be suggested that NIPP-1 has potential to be used in anti-fibrosis treatment.

• Journal of Life Science
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• v.19 no.12
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• pp.1794-1801
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• 2009

This study was conducted to examine the effects of soluble collagen peptides extract supplementation on the improvement of blood glucose, lipid components and enzyme activities in the sera of streptozotocin (STZ, 55 mg/kg BW, IP injection)-induced diabetic rats fed on experimental diets for 5 weeks. The concentrations of blood glucose, total cholesterol, atherosclerotic index, LDL, LDL-cholesterol, free cholesterol, cholesteryl ester ratio, triglycerides (TG) and phospholipids (PL) in serum were remarkably higher in the diabetic group (group SW) and STZ (IP)+collagen peptides extract supplementation group (group SFW) than those in the control group (group CG, basal diet + water). However the concentrations of blood glucose, total cholesterol, atherosclerotic index, LDL, LDL-cholesterol, free cholesterol, cholesteryl ester ratio, TG and PL in serum were lower in the SFW group than in the SW group, whereas the ratio of HDL-cholesterol concentration to total cholesterol and HDL-cholesterol concentration in the SFW group were higher than in the SW group. The activities of alkaline phosphatase (ALP) and aminotransferase (AST, ALT) in serum were lower in the SFW group than in the diabetic SW group. The results shown above suggest that soluble collagen peptides extract supplementation effectively improves blood glucose, lipid compositions and enzyme activities in the sera of STZ induced diabetic rats.