Muthukumaran N, Dhar S C
Ital J Biochem. 1983 Jul-Aug;32(4):239-53.
A glucoamylase was isolated from the culture filtrate of Rhizopus nodosus and was separated from the acid lipase by DEAE-cellulose chromatography at pH 8.0 It was purified by Concanavalin A Sepharose 4B affinity chromatography followed by CM-Sephadex chromatography 387 fold with 30.7% yield. The homogeneity of the enzyme were confirmed by polyacrylamide gel electrophoresis and immunological studies. The different physico-chemical properties of the enzyme were studied. The molecular weight of the enzyme was found to be 71,000. Ethylenediaminetetraacetic acid had no effect on the enzyme whereas Hg2+ partially inhibited the enzyme activity. Tryptophan residues were found to be essential for the enzyme activity.
从结节根霉的培养滤液中分离出一种葡糖淀粉酶，并在pH 8.0条件下通过DEAE-纤维素色谱法将其与酸性脂肪酶分离。通过伴刀豆球蛋白A琼脂糖4B亲和色谱法，随后进行CM-葡聚糖凝胶色谱法进行纯化，纯化倍数为387倍，产率为30.7%。通过聚丙烯酰胺凝胶电泳和免疫学研究证实了该酶的同质性。研究了该酶不同的物理化学性质。发现该酶的分子量为71,０００。乙二胺四乙酸对该酶没有影响，而Hg2+部分抑制酶活性。发现色氨酸残基对酶活性至关重要。
