Immobilization of thermostable β-glucosidase from Sulfolobus shibatae by cross-linking with transglutaminase

摘要: Abstract Thermostable β-glucosidase from Sulfolobus shibatae was immobilized on silica gel modified or not with 3-aminopropyl-triethoxysilane using transglutaminase as a cross-linking factor. Obtained preparations had specific activity of 3883 U/g the support, when measured at 70 °C o-nitrophenyl β- d -galactopyranoside (GalβoNp) substrate. The highest immobilization yield enzyme achieved pH 5.0 in reaction media. most active were obtained concentration 40 mg/ml 50 °C. almost completely terminated after 100 min and prolonged time this process did cause considerable changes preparations. influence considerably optimum temperature GalβoNp hydrolysis catalyzed by investigated (98 °C, 5.5). broad substrate specifity properties thermostable S. silica-gel indicate its suitability for lactose during whey processing.