Food Engineering and Technology Department, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga, Mumbai 400 019, India.
Carbohydr Polym. 2013 Oct 15;98(1):1191-7. doi: 10.1016/j.carbpol.2013.07.032. Epub 2013 Jul 20.
Two enzymes, α-amylase and glucoamylase have been individually and co-conjugated to pectin by covalent binding. Both the enzyme systems showed better thermal and pH stability over the free enzyme system with the complete retention of original activities. Mixture of individually conjugated enzymes showed lower inactivation rate constant with longer half life than the co-conjugated enzyme system. Individually conjugated enzymes showed an increase of 56.48 kJ/mole and 38.22 kJ/mole in activation energy for denaturation than the free enzymes and co-conjugated enzymes, respectively. Km as well as Vmax of individually and co-conjugated enzymes was found to be higher than the free enzymes. SDS-polyacrylamide gel electrophoresis confirmed the formation of conjugate and co-conjugate as evident by increased molecular weight. Both the enzyme systems were used for starch hydrolysis where individually conjugated enzymes showed highest release of glucose at 60 °C and pH 5.0 as compared to free and co-conjugated enzyme.
两种酶，α-淀粉酶和糖化酶已分别和共接枝到果胶通过共价键合。两个酶系统表现出更好的热和 pH 稳定性比游离酶系统具有原始活性的完全保留。混合的单独共轭酶表现出较低的失活速率常数比共共轭酶系统更长的半衰期。单独共轭酶表现出增加 56.48 kJ/mole 和 38.22 kJ/mole 的变性的活化能比游离酶和共共轭酶，分别。Km 以及 Vmax 的单独和共共轭酶被发现比游离酶高。SDS-聚丙烯酰胺凝胶电泳证实了形成的共轭和共共轭体明显增加分子量。这两种酶系统都用于淀粉水解，其中单独共轭酶在 60 °C 和 pH 5.0 下显示出最高的葡萄糖释放，与游离酶和共共轭酶相比。
