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Position: Home > Articles > Optimization of Enzymatic Hydrolysis of Amaranth Protein for Preparing Angiotensin-Ⅰ Converting Enzyme(ACE) Inhibitory Peptides by Response Surface Methodology FOOD SCIENCE 2013,34 (19) 254-260

响应面法优化酶解苋籽蛋白制备ACE抑制肽工艺

作  者：
陈飞平;周家华;常虹;曾凡坤
单  位：
西南大学食品科学学院;北京市农林科学院农业综合发展研究所
关键词：
籽粒苋;ACE抑制肽;酶解;响应面分析
摘  要：
采用响应面法优化碱性蛋白酶酶解苋籽蛋白的工艺条件,制备高活性的血管紧张素转换酶(ACE)抑制肽。通过单因素试验设计,分别考察酶种类、时间、底物质量浓度、酶与底物比、pH值和温度等因素对酶解产物水解度和ACE抑制活性的影响。采用三元二次旋转正交组合设计试验,以ACE抑制率为响应值对工艺进一步优化,经过响应面分析建立回归模型,并从模型中获得最优的酶解条件为:酶与底物比3.50%、pH8.78、温度54.4℃,在此条件下,用碱性蛋白酶在体系底物质量浓度为4g/100mL时酶解苋籽蛋白3h,得到产物的ACE抑制率为46.45%,与预测值46.63%接近,同时其抑制ACE活性的IC50为0.756mg/mL。
译  名：
Optimization of Enzymatic Hydrolysis of Amaranth Protein for Preparing Angiotensin-Ⅰ Converting Enzyme(ACE) Inhibitory Peptides by Response Surface Methodology
作  者：
CHEN Fei-ping;ZHOU Jia-hua;CHANG Hong;ZENG Fan-kun;College of Food Science,Southwest University;Institute of Agricultural Integrated Development,Beijing Academy of Agricultural and Forestry Sciences;
关键词：
amaranth;;ACE inhibitory peptide;;enzymatic hydrolysis;;response surface methodology
摘  要：
In the present study, response surface methodology was used to optimize the process conditions for the hydrolysis of amaranth protein by alcalase to prepare highly active angiotensin-I converting enzyme(ACE) inhibitory peptides. One-factorat- a-time designs were used to analyze the effect of enzyme type, hydrolysis time, substrate concentration, enzyme/substrate ratio, hydrolysis pH and hydrolysis temperature on the degree of hydrolysis(DH) and ACE inhibitory activity of amaranth protein hydrolysate. A quadratic regression model describing ACE inhibitory rate as a function of three variables was fitted by using an orthogonal rotary composite design. The optimal hydrolysis conditions were obtained from the regression model as follows: enzyme/substrate ratio of 3.50%, hydrolysis pH of 8.78, hydrolysis temperature of 54.4 ℃, substrate concentration of 4 g/100 mL and hydrolysis time of 3 h. Under these conditions, the ACE inhibitory activity of the obtained hydrolysate was 46.45%, which was close to the predicted value. At the same time, the IC50 of the hydrolysate was 0.756 mg/mL.

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