Li Jian-Ming, Wang Wen-Jun, Chen Hui, Lin Su-Yun, Mao Xin-Yi, Yu Jun-Min, Chen Ling-Li
College of Food Science and Engineering, Jiangxi Agricultural University, Nanchang 330045, China.
Food Chem X. 2024 Aug 30;23:101789. doi: 10.1016/j.fochx.2024.101789. eCollection 2024 Oct 30.
In this study, cattle bone collagen peptides-selenium chelate (CCP-Se) was prepared and its structure, oxidation resistance and stability were characterized. The selenium binding capacity was 33.65 ± 0.13 mg/g by optimized preparation conditions. Structural analysis showed that selenium ions bound mainly to the amino nitrogen, carboxyl oxygen and hydroxyl oxygen atoms of the cattle bone collagen peptide (CCP). The microstructure and particle size analyses showed that the particle size of CCP-Se was increased and formed a regular and compact crystal structure compared with CCP. Additionally, CCP-Se exhibited excellent antioxidant activity. Stability analysis showed that CCP-Se was stable in thermal processing, simulated digestion and acid/alkali tolerance tests. The intestinal selenium permeability of CCP-Se was significantly better than sodium selenite ( < 0.05). This study provides reference for the high-value application of cattle bone and suggests the potential of CCP-Se as a new effective selenium supplement.
本研究制备了牛骨胶原蛋白肽-硒螯合物（CCP-Se），并对其结构、抗氧化性和稳定性进行了表征。通过优化制备条件，硒结合能力为33.65±0.13mg/g。结构分析表明，硒离子主要与牛骨胶原蛋白肽（CCP）的氨基氮、羧基氧和羟基氧原子结合。微观结构和粒度分析表明，与CCP相比，CCP-Se的粒径增大，形成了规则致密的晶体结构。此外，CCP-Se表现出优异的抗氧化活性。稳定性分析表明，CCP-Se在热加工、模拟消化和耐酸/碱试验中均稳定。CCP-Se的肠道硒通透性显著优于亚硒酸钠（P<0.05）。本研究为牛骨的高值化利用提供了参考，并表明CCP-Se作为一种新型有效硒补充剂的潜力。
