摘要
采用转谷氨酰胺酶催化大豆蛋白与壳寡糖发生糖基化反应,制备糖基化大豆蛋白,随后用胰蛋白酶对其进行限制性酶解,制得水解度为1%、5%、10%和15%的酶解物。分析糖基化及限制性酶解对大豆蛋白的二级结构及抗氧化活性的影响。结果表明:糖基化大豆蛋白的分子发生了交联,酶解物的相对分子质量显著变小,而且分布更加广泛;糖基化大豆蛋白的结构变得无序,酶解导致大豆蛋白的无规则卷曲结构增加;两种修饰技术均能够改善大豆蛋白的抗氧化活性(DPPH自由基清除能力、还原力及亚铁离子螯合能力);糖基化及随后的酶解作用显著改变了大豆蛋白的表观黏度和黏弹特性。
The glycosylated soybean protein (GSPI) was first prepared by transglutaminase in the presence of oligochitosan and then hydrolyzed by trypsin to obtain the hydrolysates with hydrolysis degree of 1%, 5%, 10% and 15%. The effects of glycosylation and limited enzymatic hydrolysis on the secondary structure and antioxidant activities of soybean protein (SPI) were investigated. The results revealed the cross - linking of GSPI, while the hydrolysates exhibited significantly smaller relative molecular weight and wide distribution compared with SPI. GSPI structure became disorderly, and the enzymatic hydrolysis resulted in an increase of the random coil structure of SPI. The two modification technologies could improve the antioxidant activities of SPI (DPPH free radical scavenging activity, reducing power and Fe^2+ - chelating activity). The two modification methods significantly changed the apparent viscosity and viscoelastic characteristics of SPI.
出处
《中国油脂》
CAS
CSCD
北大核心
2017年第11期65-69,共5页
China Oils and Fats
基金
国家自然科学基金资助项目(31401639)
黑龙江省本科高等学校青年创新人才支持计划(UNPYSCT-2015094)
关键词
大豆分离蛋白
糖基化
限制性酶解
二级结构
抗氧化活性
soybean protein isolate
glycosylation
limited enzymatic hydrolysis
secondary structure
antioxidant activity