ISSN:
0006-3592
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
A comparative study was conducted into the immobilization of β-galactosidase, albumin, and γ-globulin on an epoxy-activated polyacrylic matrix (oxirane C, Röhm-Pharma GmbH, Darmstadt). The kinetic parameters of the immobilized β-galactosidase were investigated with three kinds of miniaturized analytical reactors: namely, stirred batch, continuous stirred-tank, and packed-bed reactors. The optimum binding conditions, saturation activity and Michaelis constant of immobilized β-galactosidase are given, together with determinations of the binding capacity of the oxirane C matrix for the three proteins investigated. For beta;-galactosidase a saturation activity of 1300 U/g oxirane C was reached. The maximum binding, achieved by experiment, was 140 mg/g with 0.69 yield for albumin, 120 mg/g with 0.61 yield for γ-globulin, and 40 mg/g with 0.42 yield for β-galactosidase. From these data the inner surface of the matrix as a function of the size of the bound proteins was estimated.
Additional Material:
13 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bit.260220112
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