De Cordt S F, Hendrickx M E, Maesmans G J, Tobback P P
Centre of Food Science and Technology, Faculty of Agricultural and Applied Biological Sciences, Katholieke Universiteit te Leuven, Belgium.
J Chem Technol Biotechnol. 1994 Feb;59(2):193-9. doi: 10.1002/jctb.280590211.
For the immobilization of Bacillus licheniformis alpha-amylase to porous glass beads, the performances of three possible linking agents, glutaric dialdehyde, benzoquinone and s-trichlorotriazine were assessed in respect of the protein yield, the enzymic activity and the thermostability of the immobilized enzyme. These three properties are to be evaluated in view of the possible use of the enzyme preparations as time-temperature-integrators (TTIs) for assessing the severity of heat pasteurization or sterilization processes of food or pharmaceuticals. All three linkers improved the enzyme's resistance to irreversible heat inactivation to a similar extent and in each case biphasic inactivation kinetics were observed, whereas the dissolved B. licheniformis alpha-amylase showed a simple first order decay. The immobilization yield, measured as protein per carrier weight, did not differ markedly for the three linkers, although the enzymic activity of the glutaric dialdehyde-linked enzyme was lower than that of the benzoquinone- and s-trichlorotriazine-linked preparations.
为了将地衣芽孢杆菌α-淀粉酶固定到多孔玻璃珠上，针对固定化酶的蛋白质产量、酶活性和热稳定性，评估了三种可能的连接剂——戊二醛、苯醌和三聚氯氰的性能。鉴于酶制剂可能用作时间-温度积分仪（TTIs）来评估食品或药品热巴氏杀菌或灭菌过程的严苛程度，需要对这三种特性进行评估。所有三种连接剂在相似程度上提高了酶对不可逆热失活的抗性，并且在每种情况下都观察到双相失活动力学，而溶解的地衣芽孢杆菌α-淀粉酶表现出简单的一级衰减。以每载体重量的蛋白质衡量的固定化产率，对于这三种连接剂而言没有显著差异，尽管戊二醛连接的酶的酶活性低于苯醌和三聚氯氰连接的制剂。
