The Immobilization of Enzymes on Nylon Structures and Their Use in Automated Analysis

Overview

Journal Biochem J

Specialty Biochemistry

Date 1972 Sep 1

PMID 4643309

Citations 3

Authors

D J Inman

W E Hornby

Affiliations

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Abstract

1. Glucose oxidase (EC 1.1.3.4) and urease (EC 3.5.1.5) were covalently attached through glutaraldehyde to low-molecular-weight nylon powder. 2. Immobilized derivatives of glucose oxidase and urease were prepared by cross-linking the respective enzymes within the matrix of a nylon membrane. 3. An improved process is described for the immobilization of glucose oxidase and urease on the inside surface of partially hydrolysed nylon tube. 4. Automated analytical procedures are described for the determination of glucose with each of the three immobilized glucose oxidase derivatives and for the determination of urea with each of the three immobilized urease derivatives. 5. The efficiencies of the three immobilized enzyme structures as reagents for the automated determination of their substrates were compared.

Citing Articles

Chemically modified nylons as supports for enzyme immobilization. Polyisonitrile-nylon.

Goldstein L, Freeman A, Sokolovsky M Biochem J. 1974; 143(3):497-509.

PMID: 4618475 PMC: 1168419. DOI: 10.1042/bj1430497a.

Preparation of some immobilized linked enzyme systems and their use in the automated determination of disaccharides.

Inman D, Hornby W Biochem J. 1974; 137(1):25-32.

PMID: 4206908 PMC: 1166076. DOI: 10.1042/bj1370025.

Detoxification of organophosphate pesticides using a nylon based immobilized phosphotriesterase from Pseudomonas diminuta.

Caldwell S, Raushel F Appl Biochem Biotechnol. 1991; 31(1):59-73.

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References

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Sundaram P, Hornby W . Preparation and properties of urease chemically attached to nylon tube. FEBS Lett. 1970; 10(5):325-327. DOI: 10.1016/0014-5793(70)80464-1. View

JANSEN E, Tomimatsu Y, Olson A . Cross-linking of -chymotrypsin and other proteins by reaction with glutaraldehyde. Arch Biochem Biophys. 1971; 144(1):394-400. DOI: 10.1016/0003-9861(71)90492-9. View

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