Purification and Characterization of Chitosanase and Exo-β-D-Glucosaminidase from a Koji Mold,Aspergillus oryzaeIAM2660 | Zendy

XiaoYong Zhang | Zendy; Anlan Dai | Zendy; Xuekun Zhang | Zendy; K Kuroiwa | Zendy; Ritsuko Kodaira | Zendy; Makoto Shimosaka | Zendy; Mitsuo Okazaki | Zendy

Open Access

Purification and Characterization of Chitosanase and Exo-β-D-Glucosaminidase from a Koji Mold,Aspergillus oryzaeIAM2660

Author(s) -

XiaoYong Zhang,

Anlan Dai,

Xuekun Zhang,

K Kuroiwa,

Ritsuko Kodaira,

Makoto Shimosaka,

Mitsuo Okazaki

Publication year - 2000

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.64.1896

Subject(s) - chitosanase , aspergillus oryzae , chitosan , chitin , enzyme , chemistry , aspergillus flavus , biochemistry , rhizopus oryzae , glucosamine , aspergillus , hydrolysis , chitinase , oligomer , microbiology and biotechnology , biology , fermentation , food science , organic chemistry

Chitosan-degrading activity was detected in the culture fluid of Aspergillus oryzae, A. sojae, and A. flavus among various fungal strains belonging to the genus Aspergillus. One of the strong producers, A. oryzae IAM2660 had a higher level of chitosanolytic activity when N-acetylglucosamine (GlcNAc) was used as a carbon source. Two chitosanolytic enzymes, 40 kDa and 135 kDa in molecular masses, were purified from the culture fluid of A. oryzae IAM2660. Viscosimetric assay and an analysis of reaction products by thin-layer chromatography clearly indicated the endo- and exo-type cleavage manner for the 40-kDa and 135-kDa enzymes, respectively. The 40-kDa enzyme, designated chitosanase, catalyzed a hydrolysis of glucosamine (GlcN) oligomers larger than pentamer, glycol chitosan, and chitosan with a low degree of acetylation (0-30%). The 135-kDa exo-beta-D-glucosaminidase,enzyme,named released a single GlcN residue from the GlcN oligomers and chitosan, but did not release GlcNAc residues from either GlcNAc oligomer or colloidal chitin.

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