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Preparation and characterization of isolubilized L ‐amino acid oxidase
Author(s) -
Weetall H. H.,
Baum G.
Publication year - 1970
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260120307
Subject(s) - chemistry , amino acid , enzyme , cysteine , leucine , substrate (aquarium) , phenylalanine , isoleucine , methionine , covalent bond , enzyme assay , d amino acid oxidase , biochemistry , asparagine , oxidase test , chromatography , organic chemistry , biology , ecology
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.