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黑豆蛋白质酶水解物体外抗氧化活性的研究
引用本文:刘恩岐,贺菊萍,陈振家,刘虎平,李玉娥. 黑豆蛋白质酶水解物体外抗氧化活性的研究[J]. 中国粮油学报, 2009, 24(11)
作者姓名:刘恩岐  贺菊萍  陈振家  刘虎平  李玉娥
作者单位:1. 徐州工程学院食品工程学院食品资源开发与利用重点建设实验室,徐州,221008
2. 山西农业大学食品科学与工程学院,太谷,030801
基金项目:山西省留学归国人员科研资助计划项目 
摘    要:采用Alcalase、Neutrase和Flavourzyme蛋白酶水解2种不同类型的黑豆蛋白,在其最适水解条件下,通过单酶水解和分阶段多酶复合水解方式制备黑豆蛋白水解物,利用邻苯三酚自氧化法测定比较其体外抗氧化活性.结果表明:在水解度相近的情况下,早熟大粒黑豆蛋白的Alcalase单酶水解物的抗氧化活性高于晚熟小粒黑豆蛋白;在水解时间相同的情况下,黑豆蛋白的Alcalase单酶水解物的抗氧化活性高于Neutrase和Flavourzyme蛋白酶;Alcalase和Neutrase分阶段水解90 min高于Alcalase单酶水解4 h的黑豆蛋白水解物的抗氧化活性;试验获得的具有较高抗氧化性的质量分数为2%的黑豆蛋白酶水解物,对邻苯三酚自氧化的抑制率与0.01%的维生素C水溶液相近.

关 键 词:黑豆蛋白  酶水解  抗氧化活性

Antioxidation Activity in vitro of Enzymic Hydrolysates from Black Soybean
Liu Enqi,He Juping,Chen Zhenjia,Liu Huping,Li Yue. Antioxidation Activity in vitro of Enzymic Hydrolysates from Black Soybean[J]. Journal of the Chinese Cereals and Oils Association, 2009, 24(11)
Authors:Liu Enqi  He Juping  Chen Zhenjia  Liu Huping  Li Yue
Abstract:The proteins of two types of black soybean were hydrolyzed by alcalase,neutrase and flavourzyme,and with single enzyme type or multi-enzyme type by stages.The antioxidation activities of the enzymic hydrolysates were compared by the pyrogallol autoxidation method.Results:The antioxidation activity of the protein of early-maturing big black soybean hydrolyzed by single alcalase is higher than that of late-maturing small black soybean in the similar DH situation.With zydrolyzation for the same time,the antioxidation activity of the protein of black soybean hydrolyzed by single alcalase is higher than that hydrolyzed by neutrase and flavourzyme individually.The antioxidation activity of black soybean protein hydrolyzed by alcalase and neutrase with multi-enzyme type by stages for 90 rain is higher than that hydrolyzed by single alcalase for 4 h.The inhibition rate against pyrogallic autoxidation of the black soybean enzymic hydrolysates in mass fraction of 2% produced in this work is comparable to that of 0.01% vitamin C.
Keywords:black soybean proteins  enzymic hydrolysate  antioxidation activity
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