Effects of carbodiimide structure on the immobilization of enzymes View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-08

AUTHORS

B. SzajÀNi, P. SÜdi, Gabriella KlamÀr, Zsuzsa M. JÀszay, I. PetnehÀzy, L. TŐke

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. More... »

PAGES

225

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf02921689

DOI

http://dx.doi.org/10.1007/bf02921689

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037126541

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1952934


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