Effects of carbodiimide structure on the immobilization of enzymes |
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Authors: | B. SzajÀNi P. SÜdi Gabriella KlamÀr Zsuzsa M. JÀszay I. PetnehÀzy L. TŐke |
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Affiliation: | Reanal Factory of Laboratory Chemicals, Budapest, Hungary. |
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Abstract: | A series of water-soluble disubstituted carbodiimides of different structure was tested for enzyme immobilization. In the experiments, a polyacrylamide-type bead polymer possessing carboxylic functional groups was used as support. The enzymes immobilized were aminoacylase (N-acylamino acid amidohydrolase; EC 3.5.1.14), arginase (L-arginine amidinohydrolase; EC 3.5.3.1), cyclodextrin glycosyltransferase (alpha-1,4-glucan 4-glycosyltransferase, cyclizing; EC 3.2.1.19), glucoamylase (1,4-alpha-D-glucan glycohydrolase, EC 3.2.1.3), and carboxypeptidase B (peptidyl-L-lysine [L-arginine] hydrolase; EC 3.4.17.2). It was found that the degree of immobilization strongly depended on the structure of carbodiimide used. |
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Keywords: | KeywordHeading" >Index Entries Water-soluble carbodiimides water-soluble carbodiimides in enzyme immobilization aminoacylase, immobilized arginase, immobilized cyclodextrin glycosyltransferase immobilized glucoamylase, immobilized carboxypeptidase B, immobilized |
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