PURIFICATION AND PROPERTIES OF A XYLANASE FROM CELLVIBRIO-GILVUS THAT HYDROLYZES PARA-NITROPHENYL CELLOOLIGOSACCHARIDES

被引：11

作者：

HAGA, K ^{[1
]}

KITAOKA, M ^{[1
]}

KASHIWAGI, Y ^{[1
]}

SASAKI, T ^{[1
]}

TANIGUCHI, H ^{[1
]}

机构：

[1] NIPPON PETROCHEM CO LTD,CHIYODA KU,TOKYO 100,JAPAN

来源：

AGRICULTURAL AND BIOLOGICAL CHEMISTRY | 1991年 / 55卷 / 08期

关键词：

D O I：

10.1080/00021369.1991.10870897

中图分类号：

S3 [农学（农艺学）];

学科分类号：

0901 ;

摘要：

An enzyme component that hydrolyzes pNP-G2 but not CMC has been isolated from a culture broth of Cellvibrio gilvus by a multi-step procedure involving Butyl-Toyopearl, DEAE-Toyopearl, and CM-Toyopearl chromatographies. The purified enzyme gave a single protein band on native, SDS-, and IEF-PAGE. The enzyme had a molecular weight of 40,000, an isoelectric point of 5.0, an optimum pH of 6.5, and an optimum temperature of 55-degrees-C. It was stable from pH 4.0 to 9.0 at 37-degrees-C for 1 hr and below 50-degrees-C for 30 min. It hydrolyzed agluconic bonds not only of pNP-G2 but also of pNP-G3, pNP-G4, and pNP-G5. Cellooligosaccharides with D.P. of 3 to 5 were not hydrolyzed at all. Instead, the enzyme hydrolyzed xylan 4 times as fast as pNP-G2. Both HgCl2 and p-chloromercuribenzoic acid inhibited the two activities completely. Xylan inhibited the hydrolysis of pNP-G2 competitively. From these results, the purified enzyme was considered to be a unique xylanase that hydrolyzed the agluconic bonds of pNP-G(n).

引用

页码：1959 / 1967

页数：9

共 17 条

[1] DETECTION OF CELLULASE ACTIVITY IN POLYACRYLAMIDE GELS USING CONGO RED-STAINED AGAR REPLICAS [J].