Montero M A, Romeu A
Department of Biochemistry and Biotechnology, University of Rovira i Virgili, Tarragona, Spain.
Biochem Mol Biol Int. 1993 Jul;30(4):685-9.
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.
冻干杏仁β-葡萄糖苷酶（EC 3.2.1.21）已被吸附到伴刀豆球蛋白A-琼脂糖凝胶（CAS）上。CAS-酶复合物制剂的酶活性单位产率为131%。游离β-葡萄糖苷酶的动力学参数值为：KM = 1.7 mM，Vmax = 330.1 U/mg蛋白质。固定化形式显示以下值：KM = 1.7 mM，Vmax = 402.6 U/mg蛋白质。两种酶形式显示出基本相同的温度和pH活性模式（最适温度：50℃，最适pH约为6.0），然而，CAS-酶复合物在pH 6时的pH稳定性明显高于游离溶液中的β-葡萄糖苷酶。
