Purification and characterization of extracellular beta-galactosidase secreted by supension cultured rice (Oryza sativa L.) cells

Satoshi Kaneko; Hideyuki Kobayashi

doi:10.1271/bbb.67.627

Purification and characterization of extracellular beta-galactosidase secreted by supension cultured rice (Oryza sativa L.) cells

Biosci Biotechnol Biochem. 2003 Mar;67(3):627-30. doi: 10.1271/bbb.67.627.

Authors

Satoshi Kaneko¹, Hideyuki Kobayashi

Affiliation

¹ National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan. sakaneko@nfri.affrc.go.jp

PMID: 12723614
DOI: 10.1271/bbb.67.627

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Chromatography, Liquid / methods
Electrophoresis, Polyacrylamide Gel
Extracellular Space / enzymology*
Galactose / analogs & derivatives
Galactose / metabolism
Hydrogen-Ion Concentration
Molecular Weight
Oryza / cytology
Oryza / enzymology*
Oryza / physiology
Substrate Specificity
Temperature
beta-Galactosidase / isolation & purification*
beta-Galactosidase / metabolism*

Substances

beta-Galactosidase
Galactose