Isolation and characterization of a beta-primeverosidase-like endo-manner beta-glycosidase from Aspergillus fumigatus AP-20.
A novel beta-glycosidase-producing microorganism was isolated from soil and identified as Aspergillus fumigatus AP-20 based on its taxonomical characteristics. The enzyme was found to be an extracellular protein in the culture of the isolated fungus and was purified 88-fold by fractionation with ammonium sulfate followed by successive column chromatographies on phenyl-Sepharose HP and Mono P HR. The molecular mass was estimated to be 47 kDa by SDS-PAGE and the isoelectric point to be pH 6.0 by isoelectric focusing. The purified enzyme was highly specific for a substrate, p-nitrophenyl beta-primeveroside (6-O-beta-D-xylopyranosyl-beta-D-glucopyranoside), which was cleaved in an endo-manner into primeverose and p-nitrophenol.
Yamamoto
Shigeru
S
Amano Enzyme Inc. Gifu R&D Center, Kakamigahara, Japan.
Okada
Masamichi
M
Usui
Taichi
T
Sakata
Kanzo
K
D001232:Aspergillus fumigatus / Q000201:enzymology*; D002852:Chromatography, Ion Exchange; D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D010940:Plant Proteins; D013379:Substrate Specificity; D014462:Ultrafiltration
D010940:Plant Proteins; D006026:Glycoside Hydrolases; C460087:beta-primeverosidase