PURIFICATION AND SOME PROPERTIES OF A LEVANASE FROM STREPTOMYCES SP-7-3

被引：20

作者：

MURAKAMI, H ^{[1
]}

MUROI, H ^{[1
]}

KURAMOTO, T ^{[1
]}

TAMURA, Y ^{[1
]}

MIZUTANI, K ^{[1
]}

NAKANO, H ^{[1
]}

KITAHATA, S ^{[1
]}

机构：

[1] MARUZEN KASEI CO LTD, ONOMICHI 722, JAPAN

来源：

AGRICULTURAL AND BIOLOGICAL CHEMISTRY | 1990年 / 54卷 / 09期

关键词：

D O I：

10.1080/00021369.1990.10870301

中图分类号：

S3 [农学（农艺学）];

学科分类号：

0901 ;

摘要：

Several microorganisms that produced levan-degrading enzyme were isolated from soil and the enzymes could be classified into several types according to the products from levan. Among these enzymes a levanase from Streptomyces sp. No. 7–3 was purified to homogeneity, shown by disc-electrophoresis. The molecular weight of the enzyme was 54,000 by SDS-polyacrylamide gel electrophoresis, and 57,000 by gel filtration. The isoelectric point of the enzyme was pH 4.7. The enzyme was most active at pH 6.5 and at 40°C, and stable up to 40°C and from pH 5.5 to pH 8.5. The enzyme hydrolyzed levan to produce levanbiose predominantly. Fructose (F, 3%) and levantriose (F3, 17%) were also produced in addition to levanbiose (F2, 80%). © 1990 by the Japan Society for Bioscience, Biotechnology, and Agrochemistry.

引用

页码：2247 / 2255

页数：9

共 24 条

[1] GEL-FILTRATION BEHAVIOUR OF PROTEINS RELATED TO THEIR MOLECULAR WEIGHTS OVER A WIDE RANGE [J].