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Preparation and characterization of isolubilized L-amino acid oxidase (1970)

Weetall, H. H. ; Baum, G.

New York, NY [u.a.] : Wiley-Blackwell

Biotechnology and Bioengineering 12 (1970), S. 399-407

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ISSN: 0006-3592

Keywords: Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: The enzyme L-amino acid oxidase of Crotalus adamanteus was covalently coupled to porous 96% silica glass particles. The insolubilized enzyme was active on several L-amino acids including: leucine, isoleucine, cysteine, phenylalanine, tryptophane, and methionine. No activity was observed with D-amino acids, L-asparagine, or L-proline. Maximum activity was observed at pH 7.8. Stability of the enzyme derivative was demonstrated by continuous operation of an enzyme column for 35 days, during which the bound enzyme oxidized over 5000 times its own weight of substrate.

Additional Material: 5 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/bit.260120307

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