热诱导对大米蛋白组分理化性质及体外消化率的影响
Heat-induced changes in the physicochemical properties and in vitro digestibility of rice protein fractions.
作者信息
Liu Kunlun, Zheng Jiabao, Chen Fusheng
机构信息
Engineering Technology Research Center for Grain and Oil Food, State Administration of Grain; College of Food Science and Technology, Henan University of Technology, Zhengzhou, 450001 China.
出版信息
J Food Sci Technol. 2021 Apr;58(4):1368-1377. doi: 10.1007/s13197-020-04648-3. Epub 2020 Jul 23.
The effects of heat treatment on protein interaction, surface hydrophobicity, protein profile, amino acid composition, and in vitro digestibility of individual rice protein fractions were investigated. Heat treatment at 100 °C for 20 min had no negative effect on essential amino acids in rice protein. Surface hydrophobicity increased significantly with the increased heat treatment temperature. Moreover, free-thiol content decreased significantly with increased temperature and time extension. Hydrophobic interactions contributed to the heat-induced interaction of glutelin and prolamin. Intramolecular disulfide linkages participated in the heat-induced interaction of all rice-protein fractions. Heat treatment had no effects on the in vitro digestibility of glutelin, globulin, and albumin. Thus, the heat-induced interactions of glutelin, globulin, and albumin were not related to their digestibility. By contrast, the formation of intramolecular disulfide bonds and hydrophobic interactions in prolamin may reduce its digestibility by strengthening protein bodies-Is.
研究了热处理对单个大米蛋白组分的蛋白质相互作用、表面疏水性、蛋白质谱、氨基酸组成和体外消化率的影响。在100℃下热处理20分钟对大米蛋白中的必需氨基酸没有负面影响。表面疏水性随热处理温度的升高而显著增加。此外，随着温度升高和时间延长，游离巯基含量显著降低。疏水相互作用导致了谷蛋白和醇溶蛋白的热诱导相互作用。分子内二硫键参与了所有大米蛋白组分的热诱导相互作用。热处理对谷蛋白、球蛋白和白蛋白的体外消化率没有影响。因此，谷蛋白、球蛋白和白蛋白的热诱导相互作用与其消化率无关。相比之下，醇溶蛋白中分子内二硫键的形成和疏水相互作用可能通过强化蛋白体而降低其消化率。
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