PURIFICATION AND PROPERTIES OF INULINASE FROM ARTHROBACTER-GLOBIFORMIS S64-1

被引：3

作者：

HARAGUCHI, K

HAYASHI, K

KASUMI, T

机构：

[1] National Food Research Institute, Ministry of Agriculture, Forestry and Fisheries, Tsukuba, Ibaraki, 305

来源：

STARCH-STARKE | 1990年 / 42卷 / 01期

关键词：

D O I：

10.1002/star.19900420109

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

A bacterium, Arthrobacter globiformis S64—1, produced an inulinase in the culture broth. The enzyme was purified 442‐fold by DEAE‐Toyopearl chromatographies. It showed maximal activity at 40°C and pH 6.5. The enzyme activity was inhibited strongly by Hg2+, Fe3+, Cu2+ and EDTA. The molecular weight of the enzyme was estimated to be 100,000 by SDS‐PAGE. The isoelctric point of the enzyme was estimated to be 4.8 by isoelectric focusing on a polyacrylamide gel. The enzyme degraded inulin through an exo‐type reaction. Copyright © 1990 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim

引用

页码：28 / 30

页数：3

共 9 条

[1] IMPROVED SPRAYING REAGENTS FOR THE DETECTION OF SUGARS ON PAPER CHROMATOGRAMS [J].