The targeted development of collagen-active peptides based on composite enzyme hydrolysis: a study on the structure–activity relationship,Food & Function

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The targeted development of collagen-active peptides based on composite enzyme hydrolysis: a study on the structure–activity relationship
Food & Function ( IF 5.1 ) Pub Date : 2023-12-01 , DOI: 10.1039/d3fo04455f
Xinnuo Hu _{1,

2} , Yanjun Yang _{1,

2} , Cuihua Chang _{1,

2} , Junhua Li _{1,

2} , Yujie Su _{1,

2} , Luping Gu _{1,

2}

Affiliation

Fish collagen, derived from sustainable sources, offers a valuable substrate for generating peptides with diverse biofunctionalities. In this study, alkaline, papain, and ginger protease were used to enzymatically hydrolyze fish skin collagen. The peptide molecular weight distribution and sequence were measured using HPLC and ICP-MS-MS, with papain/alkaline protease (AP) and papain/alkaline/ginger protease (APG) hydrolyzed samples compared. As the results showed, the incorporation of ginger protease was useful for increasing the degree of hydrolysis, with the content of <400 Da peptides increasing from 49.82% to 58.56%. The identified peptide sequence in the APG sample had more proline at the C-terminal. The peptides were separated into two components (different in molecular weight) using gel column chromatography. The molecular weight distribution, amino acid composition, ACE inhibitory activity, and fibroblast proliferation activity of the collected components were measured. In comparison, the contents of proline and hydroxyproline in the larger peptides decreased obviously after combined hydrolysis by ginger protease, reflecting the formation of a peptide sequence of smaller molecular weight containing glycine and hydroxyproline. The combined hydrolysis of ginger protease was beneficial for the improvement of the ACE inhibitory activity of the sample. However, the fibroblast proliferation activity of AP was higher than that of APG, indicating that further hydrolysis by ginger protease may destroy the hydroxyproline at the end of the peptide sequence. This study proposed a creative directional hydrolysis method and provided practical guidance for the production of collagen peptides with enhanced functional activity.

中文翻译：

基于复合酶水解的胶原蛋白活性肽的靶向开发：构效关系研究

鱼胶原蛋白源自可持续来源，为生成具有多种生物功能的肽提供了宝贵的底物。在这项研究中，使用碱性、木瓜蛋白酶和生姜蛋白酶来酶水解鱼皮胶原蛋白。使用HPLC和ICP-MS-MS测量肽的分子量分布和序列，并比较木瓜蛋白酶/碱性蛋白酶(AP)和木瓜蛋白酶/碱性/姜蛋白酶(APG)水解样品。结果表明，生姜蛋白酶的掺入有助于提高水解度，<400Da肽的含量从49.82%增加到58.56%。 APG 样品中鉴定出的肽序列在 C 端含有更多脯氨酸。使用凝胶柱色谱法将肽分离成两种组分（分子量不同）。测量收集的成分的分子量分布、氨基酸组成、ACE抑制活性和成纤维细胞增殖活性。相比之下，较大的肽经生姜蛋白酶联合水解后，脯氨酸和羟脯氨酸的含量明显下降，反映出形成了含有甘氨酸和羟脯氨酸的较小分子量的肽序列。生姜蛋白酶联合水解有利于样品ACE抑制活性的提高。但AP的成纤维细胞增殖活性高于APG，表明生姜蛋白酶的进一步水解可能会破坏肽序列末端的羟脯氨酸。该研究提出了一种创造性的定向水解方法，为生产具有增强功能活性的胶原蛋白肽提供了实践指导。

更新日期：2023-12-01

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