食品科学

• 基础研究 • 上一篇    下一篇

预处理对胶原蛋白水解和血管紧张素转化酶抑制肽段释放的影响

刘 轶,马 良,张宇昊   

  1. 1.西南大学食品科学学院,重庆 400715;2.西南大学 国家食品科学与工程实验教学示范中心,重庆 400715;
    3.农业部农产品贮藏保鲜质量安全风险评估实验室(重庆),重庆 400715
  • 出版日期:2014-11-15 发布日期:2014-11-06

Influence of Pretreatment on Enzymatic Hydrolysis of Collagen and Release of Angiotensin Converting Enzyme (ACE) Inhibitory Peptides

LIU Yi, MA Liang, ZHANG Yu-hao   

  1. 1. College of Food Science, Southwest University, Chongqing 400715, China; 2. National Food Science and Engineering
    Experimental Teaching Center, Southwest University, Chongqing 400715, China; 3. Laboratory of Quality and Safety Risk
    Assessment for Agro-products on Storage and Preservation (Chongqing), Ministry of Agriculture, Chongqing 400715, China
  • Online:2014-11-15 Published:2014-11-06

摘要:

以胰蛋白酶为工具酶,研究短时热处理、超高压处理对胶原蛋白水解和血管紧张素转化酶(angiotensinconverting enzyme,ACE)抑制肽段释放的影响。结果表明:热处理可显著促进胰蛋白酶对胶原蛋白的水解和ACE抑制活性肽段释放,超高压处理组水解物水解度(degree of hydrolysis,DH)与无处理组无显著差异,ACE抑制活性显著低于无处理组。水解物DH和ACE抑制活性关系研究显示,胰蛋白酶水解胶原蛋白过程中,水解度小于5%时,ACE抑制率随水解度呈明显上升趋势,水解度大于5%后,其上升趋势不再明显。肽谱分析进一步证明热处理可有效促进胶原蛋白的水解,超高压处理可改变胰蛋白酶作用位点。热处理组水解物序列分析显示,获得序列均来源于胶原蛋白三螺旋区域,且大部分序列都具有潜在的ACE抑制活性。说明短时热处理可以有效破坏胶原蛋白的三螺旋结构,促进ACE抑制肽段的释放。

关键词: 胰蛋白酶, 胶原蛋白, 预处理, 水解, ACE抑制活性

Abstract:

Trypsin was used to hydrolyze bovine type Ⅰ collagen with trypsin for the preparation of angiotensin converting
enzyme (ACE) inhibitory peptides. The influence of pretreatment by heating or high-pressure (HP) treatment for a short
time on the degree of hydrolysis (DH) and ACE inhibitory activity of hydrolysates was studied. Heating could improve
hydrolysis of collagen and release of ACE inhibitory peptides. HP pretreatment caused no significant difference in DH from
the untreated control, but exhibited significantly lower ACE inhibitory activity than the control. The correlation between DH
and ACE inhibition implied that ACE inhibition rose rapidly as DH increased, until reaching a plateau at a DH level of 5%.
The peptide profile showed that collagen could be hydrolyzed effectively after heating and the sites hydrolyzed by trypsin
could be changed after HP pretreatment. Sequence analysis of peptides from collagen with heating pretreatment showed
that all sequences were from the triple-helix of collagen and most of them could have strong ACE inhibitory activity, which
implied the triple-helix of collagen could be damaged and ACE inhibitory peptides could be released effectively after shorttime
heating pretreatment.

Key words: trypsin, collagen, pretreatment, hydrolysis, ACE inhibitory activity