title: Properties of almond beta-glucosidase immobilized on concanavalin A-sepharose.
abstract: Lyophylized almond beta-glucosidase (EC 3.2.1.21) has been adsorbed onto Concanavalin A-Sepharose (CAS). The yield of the enzymatic units of the CAS-enzyme complex preparation was 131%. The values of the kinetic parameters of the free beta-glucosidase were: kM = 1.7 mM and Vmax = 330.1 U/mg protein. The immobilised form showed the following values: kM = 1.7 mM and Vmax = 402.6 U/mg protein. Both enzymatic forms showed essentially the same temperature- and pH-activity patterns (temperature optimum: 50 degrees C and pH optimum approx. 6.0), however, the pH stability of the CAS-enzyme complex at pH 6 was significantly higher than the beta-glucosidase in free solution.
authors.affiliation: Department of Biochemistry and Biotechnology, University of Rovira i Virgili, Tarragona, Spain.
authors.forename: M A
authors.initials: MA
authors.lastname: Montero
authors.forename: A
authors.initials: A
authors.lastname: Romeu
mesh_terms: D004800:Enzymes, Immobilized; D005612:Freeze Drying; D006863:Hydrogen-Ion Concentration; D009754:Nuts / Q000201:enzymology*; D012685:Sepharose / Q000031:analogs & derivatives / Q000737:chemistry; D013696:Temperature; D001617:beta-Glucosidase / Q000737:chemistry* / Q000378:metabolism
chemical_list: D004800:Enzymes, Immobilized; C028326:concanavalin A-sepharose; D012685:Sepharose; D001617:beta-Glucosidase