Section 17
Chapter 16,817

Purification and properties of beta-galactosidase from Aspergillus oryzae

Tanaka, Y.; Kagamiishi, A.; Kiuchi, A.; Horiuchi, T.

Journal of Biochemistry 77(1?): 241-247


ISSN/ISBN: 0021-924X
PMID: 236999
Accession: 016816332

Beta-Galactosidase [EC] has been purified from a culture of Aspergillus oryzae by 2-propanol fractionation, column chromatography on DEAE-Sephadex A-50 and Sephadex G-200. The preparation was homogeneous on ultracentrifugation and disc electrophoresis. The enzyme showed pH optima of 4.5 with ONPG-1 as a substrate and 4.8 with lactose as a substrate. The stable pH range was from 4.0 to 9.0 and the optimum temperature was 46 degrees. The Michaelis constants were 7.2 X 10-minus 4 M with ONPG and 1.8 X 10-minus 2 M with lactose. Hg-2+, Cu-2+, N-bromosuccinimide, and sodium laurylsulfate caused marked inhibition. The apparent molecular weight was calculated to be about 105,000 by Sephadex gel filtration and sucrose density gradient centrifugation.

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