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多酚通过形成大的聚集体并减弱非共价相互作用来削弱豌豆蛋白凝胶。

Polyphenols Weaken Pea Protein Gel by Formation of Large Aggregates with Diminished Noncovalent Interactions.

机构信息

Department of Food Science and Technology, The Ohio State University, 2015 Fyffe Rd, Columbus, Ohio 43210, United States.

Research Computing, Information Technology at Purdue (ITaP), Purdue University, 155 South Grant Street, West Lafayette, Indiana 47907, United States.

出版信息

Biomacromolecules. 2021 Feb 8;22(2):1001-1014. doi: 10.1021/acs.biomac.0c01753. Epub 2021 Jan 26.

DOI:10.1021/acs.biomac.0c01753
PMID:33494594
Abstract

Polyphenols are well-known native cross-linkers and gel strengthening agents for many animal proteins. However, their role in modifying plant protein gels remains unclear. In this study, multiple techniques were applied to unravel the influence of green tea polyphenols (GTP) on pea protein gels and the underlying mechanisms. We found that the elasticity and viscosity of pea protein gels decreased with increased GTP. The protein backbone became less rigid when GTP was present based on shortened T in relaxation solid-state NMR measurements. Electron microscopy and small-angle X-ray scattering showed that gels weakened by GTP possessed disrupted networks with the presence of large protein aggregates. Solvent extraction and molecular dynamic simulation revealed a reduction in hydrophobic interactions and hydrogen bonds among proteins in gels containing GTP. The current findings may be applicable to other plant proteins for greater control of gel structures in the presence of polyphenols, expanding their utilization in food and biomedical applications.

摘要

多酚是许多动物蛋白的知名天然交联剂和凝胶增强剂。然而,它们在修饰植物蛋白凝胶中的作用尚不清楚。在这项研究中,应用了多种技术来揭示绿茶多酚(GTP)对豌豆蛋白凝胶的影响及其潜在机制。我们发现,随着 GTP 的增加,豌豆蛋白凝胶的弹性和粘度降低。基于弛豫固态 NMR 测量中 T 的缩短,发现存在 GTP 时蛋白质主链的刚性降低。电子显微镜和小角 X 射线散射表明,GTP 弱化的凝胶具有被破坏的网络结构,存在大量的蛋白质聚集体。溶剂萃取和分子动力学模拟表明,在含有 GTP 的凝胶中,蛋白质之间的疏水相互作用和氢键减少。目前的发现可能适用于其他植物蛋白,以更好地控制多酚存在下的凝胶结构,从而扩大它们在食品和生物医学应用中的使用。

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