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Position: Home > Articles > Enzymatic preparation and functional evaluation of antioxidant peptides derived from silk sericin Transactions of the Chinese Society of Agricultural Engineering 2008,24 (11) 279-283

丝胶蛋白抗氧化肽的酶法制备及功能评价

作  者:
范金波;任发政;孙雁;王芳;姜鹭
单  位:
中国农业大学食品科学与营养工程学院教育部北京市功能乳品重点实验室
关键词:
蛋白水解;水解;优化;丝胶;Alcalase;抗氧化活性;ABTS
摘  要:
为进一步开发利用废蚕丝,充分挖掘丝胶蛋白的可利用程度,该文研究了6种蛋白酶水解制备丝胶肽及产品的抗氧化活性。筛选出Alcalase碱性蛋白酶为制备丝胶抗氧化肽的理想蛋白酶,并以ABTS体系评价了丝胶肽的抗氧化活性。通过单因素试验研究了反应时间、底物浓度、反应温度、pH值、酶底物比对酶水解制备丝胶肽的影响;并通过回归正交旋转试验设计对水解条件进行优化,建立各因素与水解度和抗氧化活性的数学模型,确定Alcalase酶水解丝胶蛋白的最佳水解条件为:反应时间240min,底物浓度2%,反应温度55℃,pH8.5,酶底物比2.375%。最佳水解条件下水解度为33.35%,ABTS清除活性为43.19%。该研究为开发丝胶抗氧化肽功能产品提供了技术依据。
译  名:
Enzymatic preparation and functional evaluation of antioxidant peptides derived from silk sericin
作  者:
Fan Jinbo,Ren Fazheng,Sun Yan,Wang Fang,Jiang Lu (College of Food Science and Nutritional Engineering,China Agricultural University,The Key Laboratory of Functional Dairy of Ministry of Education and Beijing,Beijing 100083,China)
关键词:
proteolysis,hydrolysis,optimization,silk sericin,Alcalase,antioxidant activities,ABTS
摘  要:
Preparation of sericin peptide by six proteases and its antioxidant activities evaluated by ABTS system were studied.The results show that Alcalase is a perfect protease to prepare sericin peptide.Effect of hydrolysis time, substrate concentration,hydrolysis temperature,pH value and ratio(E/S)on preparation of sericin peptide with Alcalase were studied by single factor analysis.The regression models were established with factors and the indexes,including of degree of hydrolysis(DH)and antioxidant activities.The results indicate that optimal hydrolytic conditions for preparation of sericin peptide by Alcalase are as follows:hydrolytic time 240 min,substrate concentration 2%, temperature 55℃,pH value 8.5 and ratio(E/S)2.375%.Under this condition,the DH is 33.35%and ABTS scavenging activities is 43.19%.The work will be a base for development of antioxidant functional food production and provide a method for potential exploitation and utilization of silk sericin.

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