Purification and some properties of acid beta galactosidase ec 3.2.1.23 from pycnoporus cinnabarinus

Ohtakara, A.; Hayashi, N.; Mitsutomi, M.

Journal of Fermentation Technology 59(4): 325-328

1981


Accession: 006230909

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Abstract
Acid .beta.-galactosidase from P. cinnabarinus was purified by precipitation with ammonium sulfate, column chromatographies on DEAE-Sephadex A-50, CM-Sephadex C-50 and Sephadex G-100, and isoelectric focusing. The purified enzyme appeared homogeneous on disc gel electrophoresis and its MW was about 110,000. The enzyme was most active at pH 2.4, and it was stable between pH 3 and 6 (for 2 h at 37.degree. C) and below 45.degree. C (for 15 min at pH 2.4). The Km values of the enzyme were 0.95 mM for p-nitrophenyl .beta.-D-galactoside and 33 mM for lactose.