Purification and characterization of extracellular beta-galactosidase secreted by supension cultured rice (Oryza sativa L.) cells.
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.
National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan. sakaneko@nfri.affrc.go.jp
Satoshi
S
Kaneko
Hideyuki
H
Kobayashi
D002853:Chromatography, Liquid / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D005110:Extracellular Space / Q000201:enzymology*; D005690:Galactose / Q000031:analogs & derivatives / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D012275:Oryza / Q000166:cytology / Q000201:enzymology* / Q000502:physiology; D013379:Substrate Specificity; D013696:Temperature; D001616:beta-Galactosidase / Q000302:isolation & purification* / Q000378:metabolism*
D001616:beta-Galactosidase; D005690:Galactose