α-D-半乳糖苷酶源的选择及其性质的探讨  

Studies on the Activity and Property of α-D-Galactosi-dase from Different Sources

作　　者：曹志军[1] 宋世廉[1] 李玉振 

机构地区：[1]大连轻工业学院

出　　处：《食品与发酵工业》1990年第2期10-17,共8页Food and Fermentation Industries

摘　　要：本文就植物种子中α-D-半乳糖苷酶源的选择及其性质做了较详细的探讨。作者认为在相同条件下,苦杏仁、小豆和芸豆比较,小豆中的α—D—半乳糖苷酶活力最强。小豆中含有两种α—D—半乳糖苷酶(酶Ⅰ和酶Ⅱ)。本文以对—硝基苯,α—D半乳糖酶(PNPG)为底物时其最适温度和pH分别为45～50℃5.2;45℃、5.2。酶Ⅰ的V_(m a x)和Km分别为8.33μg/ml。mln和1.25×10^(-3)M,还测得元素对α—D—半乳糖苷酶有强烈的激活作用。半乳糖是酶Ⅰ的强烈竞争性抑制剂。Selection of the source of a-D-galactosidase and the studies on the nature of a-D-galactosidase were researched. The activity of a-D-galactosidase in red bean is the highest as compared with that in kidney bean and almond under the same condition. There are two kinds of a-D-galactosidase in red bean, namely EI and EH, when the substrate is PNPC, their optimum temperature and pH are 45℃-50℃, 45℃ and 5.2, 5.2 respectively, the Vmax and Km of EI are 8. 33μg/ml. min and 1.25×10-3M, saponin is a strong activator of α-D-galacto-sidase and galactose is a strong in hibitor.

关 键 词：食品酶 半乳糖苷酶 性质 酶源 选择 

分 类 号：TS201.25[轻工技术与工程—食品科学]