Virtual screening and characteristics of novel umami peptides from porcine type I collagen

被引：54

作者：

Gu, Yuxiang ^{[1
,2
,3
]}

Zhang, Jingcheng ^{[1
,2
,3
]}

Niu, Yajie ^{[1
]}

Sun, Baoguo ^{[1
,2
,3
]}

Liu, Zunying ^{[4
]}

Mao, Xiangzhao ^{[4
]}

Zhang, Yuyu ^{[1
,2
,3
]}

机构：

[1] Beijing Technol & Business Univ, Key Lab Geriatr Nutr & Hlth, Minist Educ, Beijing 100048, Peoples R China

[2] Beijing Technol & Business Univ, Food Lab Zhongyuan, Beijing 100048, Peoples R China

[3] Beijing Technol & Business Univ, Key Lab Flavor Sci China Gen Chamber Commerce, Beijing 100048, Peoples R China

[4] Ocean Univ China, Coll Food Sci & Engn, Qingdao 266100, Peoples R China

来源：

FOOD CHEMISTRY | 2024年 / 434卷

基金：

中国国家自然科学基金;

关键词：

Umami peptide; Porcine type I collagen; In silico hydrolysis; Virtual screening; Sensory evaluation; Molecular docking; TASTE;

D O I：

10.1016/j.foodchem.2023.137386

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

This study aimed to rapidly and precisely discover novel umami peptides from porcine type I collagen using virtual screening, sensory evaluation and molecular docking simulation. Porcine type I collagen was hydrolyzed in silico and six umami peptide candidates (CN, SM, CRD, GESMTDGF, MS, DGC) were shortlisted via umami taste, bioactivity, toxicity, allergenicity, solubility and stability predictions. The sensory evaluation confirmed that these peptides exhibited umami taste, with CRD, GESMTDGF and DGC displaying higher umami intensity and significant umami-enhancing effects in 0.35% sodium glutamate solution. Molecular docking predicted that Ser 276/384/385 of T1R1 and Asn68, Val277, Thr305, Ser306, Leu385 of T1R3 may also play critical roles in binding umami peptides. The umami taste of peptides may be perceived mainly through the formation of hydrogen bonds with the hydrophilic amino acids of T1R1/T1R3. This work provided a robust procedure and guidance to develop novel umami peptides from food byproducts.

引用

页数：8

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