• Title/Summary/Keyword: Collagen synthesis Fish collagen hydrolysate

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Convergence Study on Preparation of Anti-aging Peptides from Fish Collagen Hydrolysates (콜라겐 단백가수물을 이용한 항노화 펩타이드 제조에 대한 융합 연구)

  • Bae, In Young;Han, Yoo Kyung;Je, Hyun Jeong;Lee, Hyun Jun;Lee, Hyeon Gyu
    • Journal of the Korea Convergence Society
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    • v.11 no.5
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    • pp.61-72
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    • 2020
  • An anti-aging peptide was prepared from fish collagen hydrolysate (FCH) by ultrafiltration (MWCO; 1 kDa) and reversed-phased high performance liquid chromatography (RP-HPLC). Its anti-aging properties were evaluated based on the procollagen-synthesizing and MMP-1-inhibiting activities in Hs68 cells. A potent anti-aging peptide (fraction I-I) increased collagen synthesis by 46% and also inhibited MMP-1 secretion by 77%, compared with unpurified FCH. The amino acid sequence of fraction I-I was identified to be Gly-Arg-Arg-Gly-Asn-Lys (GRRGNK; the repeating Gly-X-Y sequence in collagen), and it had a molecular mass of 686.175 Da. It revealed that the anti-aging activity of GRRGNK was mainly due to skin protective effects. These results demonstrated that fish collagen hydrolysate may be a potential source of anti-aging peptides, which could be utilized in various field, including foods, cosmetics, and pharmaceuticals.

Anti-aging potential of fish collagen hydrolysates subjected to simulated gastrointestinal digestion and Caco-2 cell permeation

  • Je, Hyun Jeong;Han, Yoo Kyung;Lee, Hyeon Gyu;Bae, In Young
    • Journal of Applied Biological Chemistry
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    • v.62 no.1
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    • pp.101-107
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    • 2019
  • The objectives of this study were to evaluate the anti-aging effects and investigate the effect of simulated gastrointestinal (GI) digestion on the anti-aging properties and intestinal permeation of the potential fish collagen hydrolysates (FCH). Therefore, procollagen synthesis, matrix metalloproteinase-1 (MMP-1) production, and Caco-2 cell permeability were analyzed before and after in vitro digestion for FCHs, low-molecular weight fractions (<1 kDa), and high molecular weight fractions (>1 kDa). After being subjected to GI digestion, the level of MMP-1 inhibition was maintained, although the procollagen production was significantly (>20%) lower with all samples. Also, the digested FCHs and their <1 kDa fraction yielded 9.1 and 13.8% increased peptide transport, respectively, compared to undigested samples. Based on the effective intestinal permeation and high digestive enzyme stability, the <1 kDa fraction of FCHs is a potential bioactive material suitable for anti-aging applications in the food and cosmetics industries.