Chen Chong, Sun-Waterhouse Dongxiao, Zhang Yi, Zhao Mouming, Sun Weizheng
School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China.
School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China; School of Chemical Sciences, The University of Auckland, Auckland 1010, New Zealand; Overseas Expertise Introduction Center for Discipline Innovation of Food Nutrition and Human Health (111 Center), Guangzhou 510641, China.
Food Chem. 2020 Apr 11;323:126789. doi: 10.1016/j.foodchem.2020.126789.
Soy protein isolate (SPI) and its derived hydrolysates (SPIHs) are popular food ingredients due to their demonstrated antioxidant, stabilizing and emulsifying properties. However, little is known about the interplays among these functions. This study aimed to fill this knowledge gap through comparing the antioxidant activities in single-phase assays systems and biphasic liposomal systems of the SPIHs produced by pepsin, trypsin or alcalase with/without flavourzyme. The peptide fraction of SPIHs with molecular weight < 1 kDa generally contributed more to the detected antioxidant activity. The combination hydrolysis of flavourzyme with pepsin/trypsin/alcalase significantly influenced SPIH's reducing power and Fe chelating capacity. In liposomal systems, SPIHs influenced positively system's stability while inhibiting primary and secondary lipid oxidation products. Besides the factors affecting SPIH's antioxidant activity in the aqueous system (like amino acid composition, sequence and peptide chain length), interactions of peptides/amino acids with liposomal membrane and its lipid components also played critical roles.
大豆分离蛋白（SPI）及其衍生水解产物（SPIHs）因其已证实的抗氧化、稳定和乳化特性而成为受欢迎的食品成分。然而，对于这些功能之间的相互作用却知之甚少。本研究旨在通过比较胃蛋白酶、胰蛋白酶或碱性蛋白酶在有无风味酶作用下产生的SPIHs在单相测定系统和双相脂质体系统中的抗氧化活性，来填补这一知识空白。分子量<1 kDa的SPIHs肽段通常对检测到的抗氧化活性贡献更大。风味酶与胃蛋白酶/胰蛋白酶/碱性蛋白酶的联合水解显著影响SPIH的还原能力和铁螯合能力。在脂质体系统中，SPIHs对系统稳定性有积极影响，同时抑制初级和次级脂质氧化产物。除了影响SPIH在水相系统中抗氧化活性的因素（如氨基酸组成、序列和肽链长度）外，肽/氨基酸与脂质体膜及其脂质成分的相互作用也起着关键作用。
