State Key Laboratory of Food Science and Technology, School of Food Science and Technology , Jiangnan University , Wuxi , Jiangsu 214122 , People's Republic of China.
Department of Animal and Food Sciences , University of Kentucky , Lexington , Kentucky 40546 , United States.
J Agric Food Chem. 2018 Oct 17;66(41):10827-10834. doi: 10.1021/acs.jafc.8b03901. Epub 2018 Oct 5.
Alkaline pH shift treatment performed at varying temperatures (20-80 °C for 1, 5, and 60 min) was applied to structurally modify hemp seed protein isolate (HPI). The solubility of HPI (∼20%) was remarkably improved ( p < 0.05) with elevating the temperature and prolonging the holding time, reaching 97.5% at 80 °C for 60 min. The treated HPI exhibited a strong tendency of forming soluble large aggregates. To limit lysinoalanine (LAL) production, heating was methodically controlled to 60 °C and 5 min, where the LAL content never exceeded 100 mg/100 g of protein and the loss of cysteine and lysine was also minimal. The emulsifying activity of HPI was improved by this mild pH shift-heating combination treatment as a result of the dissociation of protein subunits, unraveling of the tertiary structure, and exposure of hydrophobic groups. Moreover, the emulsion formed by the treated protein maintained a superior stability in particle size and distribution during storage.
采用不同温度（20-80°C，1、5 和 60 分钟）的碱性 pH 值变化处理来对大麻蛋白分离物（HPI）进行结构修饰。随着温度的升高和保温时间的延长，HPI 的溶解度（约 20%）显著提高（p<0.05），在 80°C 下保温 60 分钟时达到 97.5%。处理后的 HPI 表现出强烈的形成可溶性大聚集体的趋势。为了限制赖氨酰（LAL）的产生，加热被有系统地控制在 60°C 和 5 分钟，其中 LAL 含量从未超过 100mg/100g 蛋白质，半胱氨酸和赖氨酸的损失也最小。由于蛋白质亚基的解离、三级结构的展开和疏水性基团的暴露，这种温和的 pH 值变化-加热联合处理提高了 HPI 的乳化活性。此外，经过处理的蛋白质形成的乳液在储存过程中在粒径和分布方面保持了优异的稳定性。
