Reversible immobilization of chemically modified pullulanase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-07

AUTHORS

Teresita Díaz, Ulf St»hl, Francisco Batista-Viera, Jan Carlsson

ABSTRACT

Pullulanase was provided with up to nine “de novo” thiol groups through a two-step procedure without substantially affecting its enzymatic activity. The chemically modified enzyme was immobilized via disulfide bond formation on two kinds of thiolreactive gels (pyridyldisulfide- and thiolsulfonate-substituted agarose). Thiolation of pullulanase improved both the immobilization yield and the apparent specific activity of the derivatives. More... »

PAGES

533-538

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00159572

DOI

http://dx.doi.org/10.1007/bf00159572

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1010443576


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