A novel zinc-chelating peptide identified from rapeseed (Brassica napus) protein hydrolysate: insights into its zinc-binding sites by density functional theory
文献类型： 外文期刊
作者： Wang, Hao 1 ; Huang, Jingjing 1 ; Yang, Mingliu 1 ; Zhou, Yingqin 1 ; Yin, Junfeng 1 ; Yan, Yan 1 ; Xie, Ningning 1 ;
作者机构： 1.Anhui Acad Agr Sci, Inst Agroprod Sci & Technol, Hefei 230031, Peoples R China
2.Anhui Engn Lab Funct Microorganisms & Fermented Fo, Hefei 230031, Peoples R China
3.Zhejiang Ocean Univ, Sch Food & Pharm, Zhoushan 316022, Peoples R China
关键词： Binding site; geometric structure; quantum chemistry; rapeseed protein; zinc chelating peptide
期刊名称：INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY （ 2022影响因子：3.3； 五年影响因子：3.5 ）
ISSN： 0950-5423
年卷期： 2023 年
收录情况： SCI
摘要： The binding sites between zinc chelating peptide (ZCP) and zinc have not been clearly understood at the quantum chemistry level. Ala-Ser-His (ASH), a new ZCP located in the cruciferin precursor, was identified from in vitro digestion hydrolysate of rapeseed (Brassica napus) protein. Also, ASH exerted the concentration value of 114.09 & PLUSMN; 0.98 mM showing 50% zinc chelating activity. The prepared ASH-Zn (ZCP-zinc chelate), displayed varying characteristics from ASH on surface microstructures, X-ray photon energies, and infrared spectrum. The geometric structure of ASH-Zn with minimum free energy was obtained using density functional theory, producing a bridge bond of O-21-Zn-41-O-32 between Ser and His residues. Based on the basic set of 6-311++G (d, p), O-21-Zn (41) and O-32-Zn-41, respectively, had bond lengths of 1.96503 & ANGS; and 1.94515 & ANGS;, while O-21-Zn-41-O-32 displayed a bond angle of 136.41069 & DEG;. These findings further promote research on rapeseed proteins providing new possibilities for studying peptide-metal chelates.
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