摘要
黑曲霉(AspergilluS niger)AS 3.3883所产果胶酶经DEAE Sephadex A50及Sephadex G100柱层析分离出电泳纯的两种聚半乳糖醛酸酶(PG1,PG2),并对它们的性质及结构进行了比较研究。结果证明两种酶作用的最适条件、动力学性质、分子量、氨基酸组成及金属离子对酶活力影响等方面有很大差异,但二者的每个摩尔的活力及酶的构象很相似。
Two types of polygalacturonases (PG1 and PG2) were separated and purified by DEAE-Sephadex A50 and Sephadex G100 from crude pectinase produced from A. niger AS 3.3883. Some properties and structures were investigated with purified enzyme of PGl and PG2. The results indicate that the optimum conditions of their activity, kinetic parameters, molecular weight, composition of amino acids and the effects of some metal ions on activity of the enzymes are markedly different from each other, while the molar activity and the conformations of the two types, of PG are similar.
出处
《微生物学报》
CAS
CSCD
北大核心
1995年第5期346-352,共7页
Acta Microbiologica Sinica
关键词
聚半乳糖醛酸酶
性质
结构
提纯
Polygalacturonase, Purification, Characterization
