Bioscience, Biotechnology and Biochemistry 2003-Mar
Purification and characterization of extracellular beta-galactosidase secreted by supension cultured rice (Oryza sativa L.) cells.
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Resum
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.
