PMID: 8611759Dec 1, 1995Paper

Purification and some properties of alpha-galactosidase from Penicillium purpurogenum

Bioscience, Biotechnology, and Biochemistry
H ShibuyaI Kusakabe

Abstract

alpha-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 67 kDa and 4.1, respectively. The N-terminal amino acid sequence of the enzyme was analyzed and aligned with those of other alpha-galactosidases. In addition, the enzyme acted on the stubbed alpha-galactosyl residue connected to the beta-1,4-manno-oligosaccharide chain, indicating that this specificity was quite different from that of Mortierella vinacea alpha-galactosidase.

Citations

Oct 8, 2009·Bioscience, Biotechnology, and Biochemistry·Zui FujimotoHideyuki Kobayashi
Mar 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·M FoucaultP Gouet
Mar 27, 2003·The Journal of Biological Chemistry·Zui FujimotoHiroshi Mizuno
Sep 3, 1999·Applied and Environmental Microbiology·O FridjonssonR Mattes
Oct 31, 1998·Applied and Environmental Microbiology·H ShibuyaH Kobayashi
Feb 17, 1998·Enzyme and Microbial Technology·E LuonteriL Viikari
Nov 9, 2002·Phytochemistry·Wook-Dong KimHideyuki Kobayashi

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