Literature DB >> 435616

Enzyme immobilization by radiation-induced polymerization of hydrophobic glass-forming monomers at low temperatures.

I Kaetsu, M Kumakura, M Yoshida.   

Abstract

Enzyme immobilization was studied by means of radiation-induced polymerization of hydrophobic glass-forming monomers at low temperatures. The polymerized hydrophobic composite was generally obtained in microspheric form. Enzymatic activity showed little decrease with repeated use in these systems. The particle size of the microsphere increased with increasing monomer concentration, and activity yield had a maximum at an optimum monomer concentration. Immobilization by copolymerization of hydrophilic and hydrophobic comonomers was also investigated and a maximum activity yield was found at a certain monomer concentration. A model scheme for immobilization at low temperatures was proposed and discussed.

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Year:  1979        PMID: 435616     DOI: 10.1002/bit.260210509

Source DB:  PubMed          Journal:  Biotechnol Bioeng        ISSN: 0006-3592            Impact factor:   4.530


  2 in total

1.  Radiation-induced polymerization for the immobilization of penicillin acylase.

Authors:  E Boccù; M Carenza; S Lora; G Palma; F M Veronese
Journal:  Appl Biochem Biotechnol       Date:  1987-06       Impact factor: 2.926

2.  Immobilization of antibodies and enzyme-labeled antibodies by radiation polymerization.

Authors:  M Kumakura; I Kaetsu; M Suzuki; S Adachi
Journal:  Appl Biochem Biotechnol       Date:  1983-04       Impact factor: 2.926

  2 in total

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