Purification and Some Properties of [alpha]-Galactosidase from Penicillium purpurogenum

α-Galactosidase was purified by ion-exchange chromatographies on DEAE-cellulose and SE-cellulose columns from the culture filtrate of Penicillium purpurogenum No. 618. The final preparation was judged homogeneous by SDS-PAGE and its molecular mass and isoelectric Point were estimated to be 67kDa and...

Full description

Saved in:
Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1995-12, Vol.59 (12), p.2333
Main Authors: Shibuya, Hajime, Kobayashi, Hideyuki, Park Gun, Gwi, Komatsu, Yoko, Sato, Taku, Kaneko, Reiji, Nagasaki, Hiroaki, Yoshida, Shigeki, Kasamo, Kunihiro, Kusakabe, Isao
Format: Article
Language:English
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:α-Galactosidase was purified by ion-exchange chromatographies on DEAE-cellulose and SE-cellulose columns from the culture filtrate of Penicillium purpurogenum No. 618. The final preparation was judged homogeneous by SDS-PAGE and its molecular mass and isoelectric Point were estimated to be 67kDa and 4. 1, respectively. The N-terminal amino acid sequence of the enzyme was analyzed and aligned with those of other α-galactosidases. In addition, the enzyme acted on the stubbed α-galactosyl residue connected to the β-1, 4-manno-oligosaccharide chain, indicating that this specificity was quite different from that of Mortierella vinacea α-galactosidase.
ISSN:0916-8451
1347-6947