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海蜇胶原蛋白肽-钙螯合物的结构、抗氧化活性及稳定性研究

Structural, antioxidant activity, and stability studies of jellyfish collagen peptide-calcium chelates.

作者信息

Gao Jiajia, Ning Chong, Wang Mingxia, Wei Mingming, Ren Yifei, Li Weixuan

机构信息

College of Light Industry, Liaoning University, Shenyang 110036, PR China.

出版信息

Food Chem X. 2024 Jul 31;23:101706. doi: 10.1016/j.fochx.2024.101706. eCollection 2024 Oct 30.

Abstract

The aim of this study was to prepare and characterize jellyfish collagen peptide (JCP)-calcium chelates (JCP-Ca) using peptides with different molecular weights. Further analysis revealed that the low-molecular-weight jellyfish collagen peptide (JCP1) had a higher chelation rate. Structural characterization showed that functional groups such as N-H, C[bond, double bond]O, and -COO were involved in the formation of JCP-Ca, which shifted towards a more ordered and regular structure, and smaller-molecular-weight peptides were more likely to form a denser structure. In addition, JCPs chelated with calcium ions showed excellent antioxidant capacity. JCP-Ca showed good stability in heat-treated and gastrointestinal environments, whereas the antioxidant activity was significantly reduced under highly acidic conditions. The present study addresses the knowledge gap regarding the physicochemical properties of JCP-Ca and establishes a solid research foundation for its associated products.

摘要

本研究的目的是使用不同分子量的肽制备并表征海蜇胶原蛋白肽(JCP)-钙螯合物(JCP-Ca)。进一步分析表明,低分子量海蜇胶原蛋白肽(JCP1)具有更高的螯合率。结构表征显示,诸如N-H、C=O和-COO等官能团参与了JCP-Ca的形成,其结构向更有序和规则的方向转变,且分子量较小的肽更有可能形成致密结构。此外,与钙离子螯合的JCP表现出优异的抗氧化能力。JCP-Ca在热处理和胃肠道环境中表现出良好的稳定性,而在高酸性条件下抗氧化活性显著降低。本研究填补了关于JCP-Ca物理化学性质的知识空白,并为其相关产品奠定了坚实的研究基础。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/567c/11345935/4a36cbe8ea21/gr1.jpg

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