Stabilization of a formate dehydrogenase by covalent immobilization on highly activated glyoxyl-agarose supports

Biomacromolecules

Volumn 7, Issue 3, 2006, Pages 669-673

  Bolivar, Juan M ^a   Wilson, Lorena ^a,b   Ferrarotti, Susana Alicia ^a,c   Fernandez Lafuente, Roberto ^a   Guisan, Jose M ^a   Mateo, Cesar ^a  

^a CSIC   (Spain)

^b PONTIFICIA UNIVERSIDAD CATÓLICA DE VALPARAÍSO   (Chile)

^c DEPARTAMENTO DE CIENCIAS BÁSICAS   (Argentina)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME IMMOBILIZATION; ENZYMES; HYDROPHOBICITY; INTERFACES (MATERIALS); ORGANIC SOLVENTS; PH EFFECTS; THERMAL EFFECTS;

FORMATE DEHYDROGENASE (FDH); HIGHLY ACTIVATED GLYOXLY AGAROSE; HYDROPHOBIC INTERFACES;

BIOCHEMISTRY;

AGAROSE; DEXTRAN; FORMATE DEHYDROGENASE; GLUTARALDEHYDE; GLYOXYLIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE; ORGANIC SOLVENT; POLYETHYLENEIMINE;

ACIDITY; ARTICLE; BIOCATALYST; CHEMICAL INTERACTION; CONTROLLED STUDY; COVALENT BOND; DISSOCIATION; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME IMMOBILIZATION; ENZYME INACTIVATION; ENZYME MECHANISM; ENZYME STABILITY; ENZYME SUBUNIT; HIGH TEMPERATURE; HYDROPHOBICITY; MEMBRANE REACTOR; PH; POROSITY; PRIORITY JOURNAL; PROCESS OPTIMIZATION; PROTEIN QUATERNARY STRUCTURE; TEMPERATURE; THERMOSTABILITY;

BIOCOMPATIBLE MATERIALS; CATALYSIS; DEXTRANS; ENZYMES, IMMOBILIZED; FORMATE DEHYDROGENASES; GLYOXYLATES; HYDROGEN-ION CONCENTRATION; MACROMOLECULAR SUBSTANCES; NAD; PROTEIN STRUCTURE, QUATERNARY; PSEUDOMONAS; SEPHAROSE; SOLVENTS; TEMPERATURE;

EID: 33645509894     PISSN: 15257797     EISSN: None     Source Type: Journal    
DOI: 10.1021/bm050947z     Document Type: Article

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