Gao Jiajia, Ning Chong, Wang Mingxia, Wei Mingming, Ren Yifei, Li Weixuan
College of Light Industry, Liaoning University, Shenyang 110036, PR China.
Food Chem X. 2024 Jul 31;23:101706. doi: 10.1016/j.fochx.2024.101706. eCollection 2024 Oct 30.
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.
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。