Purification and Characterization of an Endo-Polygalacturonase fromAspergillus awamori

1 January 2000

journal article
Published by Oxford University Press (OUP) in Bioscience, Biotechnology, and Biochemistry

Vol. 64 (8) , 1729-1732
https://doi.org/10.1271/bbb.64.1729

Abstract

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.

Keywords

This publication has 0 references indexed in Scilit: