Effect of combined ultrasonic and alkali pretreatment on enzymatic preparation of angiotensin converting enzyme (ACE) inhibitory peptides from native collagenous materials

被引:38
作者
Zhang, Yuhao [1 ]
Ma, Liang [1 ]
Cai, Luyun [2 ]
Liu, Yi [1 ]
Li, Jianrong [1 ,2 ]
机构
[1] Southwest Univ, Coll Food Sci, Chongqing 400716, Peoples R China
[2] Bohai Univ, Coll Food Sci & Technol, Food Safety Key Lab Liaoning Prov, Jinzhou 121013, Peoples R China
基金
中国国家自然科学基金; 中国博士后科学基金;
关键词
Ultrasonic and alkali; Pretreatment; ACE-inhibitory peptides; Native collagenous materials; SPONTANEOUSLY HYPERTENSIVE-RATS; RESPONSE-SURFACE METHODOLOGY; IN-VITRO; BOVINE COLLAGEN; SKIN; GELATIN; HYDROLYSATE; PROTEIN; OPTIMIZATION; PEPSIN;
D O I
10.1016/j.ultsonch.2016.11.008
中图分类号
O42 [声学];
学科分类号
070206 ; 082403 ;
摘要
The combined effect of ultrasonic and alkali pretreatment for the hydrolysis of native collagenous materials and release of ACE inhibitory peptides was investigated. The ultrasonic and alkali pretreatment of pig skin could accelerate the release of the ACE inhibitory peptides from the triple helix of collagen in early stages of hydrolysis. Furthermore, the pretreatment could also accelerate collapse of the triple helix and release more ACE inhibitory peptides during hydrolysis than collagen samples left untreated. Compared to untreated and alkali pretreated samples, the ultrasonic and alkali pretreatment could decrease the thermostability of pig skin significantly (P < 0.05) because the ultrasonic and alkali pretreatment could weaken hydrogen bonds and break parts of covalent bonds in collagen, leading to damage of the triple helical structure in collagen. Therefore, the ultrasonic and alkali pretreatment could damage the triple helical structure of collagen in native collagenous materials and expose more inner sites for subsequent hydrolysis, and it could be a potential way to prepare ACE inhibitory peptides effectively from collagen-rich raw material. (C)2016 Elsevier B.V. All rights reserved.
引用
收藏
页码:88 / 94
页数:7
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