Titlebook: Immobilized Biocatalysts; An Introduction Winfried Hartmeier Book 1988 Springer-Verlag Berlin Heidelberg 1988 Glucose.translation.yeast.wat

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Uses in Basic Researchy of the examples described below, the binding of the enzymes to carriers makes it possible to expose them to a succession of different media. With soluble enzymes, however, an extremely laborious procedure is necessary for separating a reaction product from the enzyme protein. Another argument in f

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Construction and Use of a Biochemical Electrode for Assaying Glucose constructed. From a series of measurements in which the parameters are glucose concentration and measuring time, it is intended to obtain values indicating the range of sensitivity and the response time of the enzyme electrode.

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Immobilization of L-Asparaginase in Nylon Microcapsulesicroencapsulation of L-asparaginase by boundary-layer polymerization, will show that satisfactory yields of activity can be obtained by this method. At the same time it will become clear that the relative difficulty of the encapsulation procedure and the lability of the microcapsules are considerabl

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General Principleslowering the energy of activation, without themselves appearing in the reaction products. In this, and in the fact that the catalyst itself is not used up, the action of enzymes resembles that of inorganic catalysts.

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Characteristics of Immobilized Biocatalystse Fig. 32), in which activity is plotted against temperature. Often, the activity is not given in international units but as the relative activity, i.e., the quotient of the actual activity and the highest activity measured.

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Application in Analytical Procedures. The method exploits the property of certain reactants to recognize each other and to form complexes. Affinity of this kind exists between antigens and antibodies, hormones and receptor proteins, to mention only two examples. As Table 20 shows, enzymes, too, have a specific affinity for a variety of substances.