Isolation and Characterization of A β-Primeverosidase-like endo-manner β-Glycosidase fromAspergillus fumigatusAP-20 | Zendy

Shigeru Yamamoto | Zendy; Masamichí Okada | Zendy; Taichi Usui | Zendy; Kanzo Sakata | Zendy

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Isolation and Characterization of A β-Primeverosidase-like endo-manner β-Glycosidase fromAspergillus fumigatusAP-20

Author(s) -

Shigeru Yamamoto,

Masamichí Okada,

Taichi Usui,

Kanzo Sakata

Publication year - 2002

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.66.801

Subject(s) - isoelectric point , aspergillus fumigatus , isoelectric focusing , glycoside hydrolase , molecular mass , enzyme , ammonium sulfate , chromatography , chemistry , biochemistry , aspergillus , fractionation , biology , microbiology and biotechnology

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.

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