PURIFICATION AND SOME PROPERTIES OF A NEW LEVANASE FROM BACILLUS SP NO 71

被引：24

作者：

MURAKAMI, H ^{[1
]}

KURAMOTO, T ^{[1
]}

MIZUTANI, K ^{[1
]}

NAKANO, H ^{[1
]}

KITAHATA, S ^{[1
]}

机构：

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

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1992年 / 56卷 / 04期

关键词：

D O I：

10.1271/bbb.56.608

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A levanase from Bacillus sp. was purified to a homogeneous state. The enzyme had a molecular weight of 135,000 and an isoelectric point of pH 4.7. The enzyme was most active at pH 6.0 and 40-degrees-C, stable from pH 6.0 to 10.0 for 20 hr of incubation at 4-degrees-C and up to 30-degrees-C for 30 min of incubation at pH 6.0. The enzyme activity was inhibited by Ag+, Hg2+, Cu2+, Fe3+, Pb2+, and p-chloroMeTCuribenzoic acid. The enzyme hydrolyzed levan and phlein endowise to produce levanheptaose as a main product. The limit of hydrolysis of levan and phlein were 71% and 96%, respectively.

引用

页码：608 / 613

页数：6

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