Purification and Characterization of an Endo-Polygalacturonase fromAspergillus awamori
Copyright policy )Purification and Characterization of an Endo-Polygalacturonase fromAspergillus awamori
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.
Molecular Sequence Data, Temperature, polygalacturonase, Hydrogen-Ion Concentration, Chromatography, Ion Exchange, Molecular Weight, Aspergillus, Polygalacturonase, pH regulation, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Amino Acid Sequence, Isoelectric Point, <i>Aspergillus awamori</i>
Molecular Sequence Data, Temperature, polygalacturonase, Hydrogen-Ion Concentration, Chromatography, Ion Exchange, Molecular Weight, Aspergillus, Polygalacturonase, pH regulation, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Amino Acid Sequence, Isoelectric Point, <i>Aspergillus awamori</i>
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