Purification and characterization of an endo-polygalacturonase from Aspergillus awamori

被引：17
|
作者：
Nagai, M
Katsuragi, T
Terashita, T
Yoshikawa, K
Sakai, T
机构：
[1] Kinki Univ, Fac Agr, Dept Food Sci & Nutr, Nara 6318505, Japan
[2] Inst Sci & Technol, Grad Sch Biol Sci, Nara 6300101, Japan
来源：
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2000年 / 64卷 / 08期
关键词：
polygalacturonase; Aspergillus awamori; pH regulation;
D O I：
10.1271/bbb.64.1729
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：
An extracellular endo-polygalacturonase (PGase) produced by Aspergillus awamori IFO 4033 was isolated from the culture filtrate. The enzyme was purified to a homogeneous preparation with cation-exchange and size-exclusion chromatographies. Its properties were investigated, comparing them with that of recombinant pgx2 gene product, a PGase having protopectinase activity. This enzyme was a monomeric protein of 41 kDa, with an isoelectric point of pH 6.1. The characteristics of this PGase substantially coincide, with that of recombinant pgx2 gene product, and the PGase is assumed to be native pgx2 gene product. The production of PGase-X2 was confirmed to be regulated by ambient pHs.
引用
收藏
页码：1729 / 1732
页数：4
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