Study On The Preparation And Activity Of Tilapia Skin Collagen Antihypertensive Enzymatic Hydrolyzate
Keywords
Tilapia Skin, Collagen, Complex Enzymatic Hydrolysis, Isolation And Purification, Angiotensin-Converting Enzyme
Abstract
This article studied the process conditions for the preparation of angiotensin-converting enzyme inhibitor (ACEI) by hydrolyzing tilapia skin collagen with single enzymes and multiple enzymes. The optimal enzymatic hydrolysis conditions for bromelain and Alcalase2.4L protease to hydrolyze fish skin collagen alone were determined through orthogonal experiments. The optimal enzymatic hydrolysis temperature, pH, enzyme/substrate, time and substrate concentration of bromelain and Alcalase2.4L protease are 45¡æ, pH4.5, 4000U/g, 4h, 6% and 55¡æ, pH7.5 respectively. ,6000¦Ì/g,2h,4%. On the basis of single enzyme hydrolysis, a composite enzyme hydrolysis experiment was carried out. The results showed that the effect was better if bromelain was first used for hydrolysis and then Alcalase2.4L protease was used for hydrolysis. Using this dual-enzyme composite hydrolysis process, the degree of hydrolysis of the hydrolyzate obtained was 30.43%, and the inhibition rate of ACE in vitro reached 68.6%. The enzymatic hydrolyzate was separated and purified using SephadexG-25 and HPLC separation methods, and components with high inhibitory activity were obtained. The IC50 of the obtained hydrolyzed stock solution and the high-activity component obtained by passing SephadexG-25 through the column were 2.82 mg/ml and 0.65 mg/ml respectively.
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Original research was done by Diao Shiqiang, Wu Yanyan, Zeng Mingyong, Li Laihao, Yang Xianqing, Chen Shengjun
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