食品科学

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响应面法优化酶解苋籽蛋白制备ACE抑制肽工艺

陈飞平1,2,周家华2,*,常 虹2,曾凡坤1   

  1. 1.西南大学食品科学学院,重庆 400715;2.北京市农林科学院农业综合发展研究所,北京 100097
  • 出版日期:2013-10-15 发布日期:2013-09-27
  • 通讯作者: 周家华

Optimization of Enzymatic Hydrolysis of Amaranth Protein for Preparing Angiotensin-Ⅰ Converting Enzyme (ACE) Inhibitory Peptides by Response Surface Methodology

CHEN Fei-ping1, 2,ZHOU Jia-hua2,*,CHANG Hong2,ZENG Fan-kun1   

  1. 1. College of Food Science, Southwest University, Chongqing 400715, China;
    2. Institute of Agricultural Integrated Development, Beijing Academy of Agricultural and Forestry Sciences, Beijing 100097, China
  • Online:2013-10-15 Published:2013-09-27
  • Contact: ZHOU Jia-hua

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。

关键词: 籽粒苋, ACE抑制肽, 酶解, 响应面分析

Abstract:

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.

Key words: amaranth, ACE inhibitory peptide, enzymatic hydrolysis, response surface methodology

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