Purification and characterization of an endo-polygalacturonase from Aspergillus awamori

Citation
M. Nagai et al., Purification and characterization of an endo-polygalacturonase from Aspergillus awamori, BIOS BIOT B, 64(8), 2000, pp. 1729-1732
Citations number
24
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Agricultural Chemistry","Biochemistry & Biophysics
Journal title
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
ISSN journal
0916-8451 → ACNP
Volume
64
Issue
8
Year of publication
2000
Pages
1729 - 1732
Database
ISI
SICI code
0916-8451(200008)64:8<1729:PACOAE>2.0.ZU;2-4
Abstract
An extracellular endo-polygalacturonase (PGase) produced by Aspergillus awa mori IFO 4033 was isolated from the culture filtrate. The enzyme was purifi ed to a homogeneous preparation with cation-exchange and size-exclusion chr omatographies. Its properties were investigated, comparing them with that o f recombinant pgx2 gene product, a PGase having protopectinase activity. Th is enzyme was a monomeric protein of 41 kDa, with an isoelectric point of p H 6.1. The characteristics of this PGase substantially coincide, with that of recombinant pgx2 gene product, and the PGase is assumed to be native pgx 2 gene product. The production of PGase-X2 was confirmed to be regulated by ambient pHs.