PURIFICATION AND PROPERTIES OF AN ALPHA-L-ARABINOFURANOSIDASE FROM COTYLEDONS OF SOYBEAN SEEDLINGS

被引：11

作者：

HATANAKA, H

IMAOKA, H

TAJIMA, S

KASAI, T

机构：

[1] ENVIRONM DEPT,TAKAMATSU CITY OFF,TAKAMATSU 760,JAPAN

[2] KAGAWA UNIV,FAC AGR,DEPT BIORESOURCE SCI,MIKI,KAGAWA 76107,JAPAN

来源：

AGRICULTURAL AND BIOLOGICAL CHEMISTRY | 1991年 / 55卷 / 10期

关键词：

D O I：

10.1080/00021369.1991.10871006

中图分类号：

S3 [农学（农艺学）];

学科分类号：

0901 ;

摘要：

An alpha-L-arabinosidase (alpha-L-arabinofuranoside arabinofuranohydrolase, EC 3.2.1.55) that can degrade both purified water soluble polysaccharide from soybean seeds and p-nitrophenyl-alpha-L-arabinofuranoside was purified 453-fold to near homogeneity from cotyledons of 4-day-old soybean seedlings. The optimum pH and K(m) against p-nitrophenyl-alpha-L-arabinofuranoside of the purified enzyme were 4.8 and 0.53 mM, respectively. The enzyme was activated by Ca2+ and Zn2+ ions, but Cu2+, Hg2+, EDTA, and L-arabonic-gamma-lactone inhibited the enzyme activity. The molecular weight of the enzyme subunit was estimated to be 87,000 by SDS-PAGE.

引用

页码：2599 / 2605

页数：7

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