Purification and Characterization of Extracellular β-Galactosidase Secreted by Supension Cultured Rice (Oryza sativaL.) Cells
Author(s) -
Satoshi Kaneko,
Hideyuki Kobayashi
Publication year - 2003
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.67.627
Subject(s) - oryza sativa , extracellular , enzyme , galactose , biochemistry , sepharose , chemistry , chromatography , biology , gene
A beta-galactosidase was purified 1300-fold by lactosyl-Sepharose 4B and Sephacryl S-200 column chromatographies from the cultured medium of a rice-cell suspension. The purified enzyme appeared as 47 kD and 40 kD polypeptides on SDS-PAGE and had a specific activity of 65.1 units/mg. Optimum activity was observed at pH 3.5 and 60 degrees C. The enzyme released galactose from galactoxyloglucan and pectic galactans.
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