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Silver Carp (Hypophthalmichthys molitrix) Scales Collagen Peptides (SCPs): Preparation, Whitening Activity Screening and Characterization

文献类型： 外文期刊

作者： Zu, Xiao-Yan 1 ; Li, Mei-Jin 1 ; Xiong, Guang-Quan 1 ; Cai, Jun 2 ; Liao, Tao 1 ; Li, Hai-Lan 1 ;

作者机构： 1.Hubei Acad Agr Sci, Inst Agroprod Proc & Nucl Agr Technol, Key Lab Cold Chain Logist Technol Agroprod, Minist Agr & Rural Affairs,Inst Agroprod Proc & Nu, Wuhan 430064, Peoples R China

2.Hubei Univ Technol, Hubei Prov Cooperat Innovat Ctr Ind Fermentat, Key Lab Fermentat Engn,Minist Educ, Hubei Key Lab Ind Microbiol, Wuhan 430068, Peoples R China

关键词： scale; collagen peptide; whitening; characterization; identification

期刊名称：FOODS （ 影响因子：5.2； 五年影响因子：5.5 ）

ISSN：

年卷期： 2023 年 12 卷 7 期

页码：

收录情况： SCI

摘要： This study involves the preparation of scale collagen peptides (SCPs) with whitening activity from silver carp (Hypophthalmichthys molitrix) and their characterization and peptide sequence identification. In this article, scanning electron microscopy (SEM) was used to observe structure changes of sliver carp scales; enzymatic hydrolysis was optimized through protease screening and response surface optimization. The ultrafiltration was used to separate SCPs and the whitening activity was comprehensively evaluated using radical scavenging rate and tyrosinase-inhibiting activity, among others. An optimal component was characterized and identified using various modern spectral analysis techniques. The results showed that the surface of silver carp scales after decalcification was smooth and clear. The pepsin had the highest peptide yield and tyrosinase-inhibiting activity (90.01% and 82.25%, respectively). The optimal enzymatic hydrolysis conditions were an enzyme dosage of 16.1%, a solid-liquid ratio of 1:15.6 and a time of 4.9 h. The proportions of hydrophobic and basic amino acids in the peptide composition were 32.15% and 13.12%, respectively. Compared with SCPs2, SCPs1 (6096.68-9513.70 Da) showed better center dot OH scavenging ability, tyrosinase-inhibiting activity and moisture absorption. SCPs1 was a macromolecular fragment of type I collagen with a triple helix structure, containing three peptide sequences with the potential for tyrosinase activity inhibition (AGPPGADGQTGQRGE, SGPAGIAGPAGPRGPAGPNGPPGKD and KRGSTGEQGSTGPLGMRGPRGAA). These results show that SCPs1 is a collagen peptide product with whitening potential.

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