The coimmobilization of D-amino acid oxidase and catalase enables the quantitative transformation of D-amino acids (D-phenylalanine) into α-keto acids (phenylpyruvic acid)

Enzyme and Microbial Technology

Volumn 23, Issue 1-2, 1998, Pages 28-33

  Fernández Lafuente, Roberto ^a   Rodriguez, Verónica ^a   Guisán, Jose M ^a   Guisán, José M ^a  

^a CSIC   (Spain)

Author keywords

Catalase; Coimmobilization; Hydrogen peroxide elimination; Oxidases; Resolution of racemic mixtures

Indexed keywords

AMINO ACIDS; BIOCONVERSION; CATALYSIS; CATALYST ACTIVITY; CATALYST DEACTIVATION; COMPOSITION EFFECTS; DERIVATIVES; HYDROGEN PEROXIDE; OXIDATION; POROUS MATERIALS; SOLUBILITY; SUBSTRATES;

CATALYZE; OXIDASE; PHENYLALANINE; PHENYLPYRUVIC ACID;

ENZYME IMMOBILIZATION;

2 OXOACID; AMINO ACID OXIDASE; CATALASE; DEXTRO AMINO ACID; HYDROGEN PEROXIDE;

ARTICLE; ENZYME IMMOBILIZATION; HYDROPHOBICITY; OXIDATION; RACEMIC MIXTURE; STEREOCHEMISTRY;

EID: 0032126831     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(98)00028-3     Document Type: Article

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