The slow-down of the CALB immobilization rate permits to control the inter and intra molecular modification produced by glutaraldehyde

Process Biochemistry

Volumn 47, Issue 5, 2012, Pages 766-774

  Barbosa, Oveimar ^a   Torres, Rodrigo ^a   Ortiz, Claudia ^a   Fernandez Lafuente, Roberto ^b  

^a UNIVERSIDAD INDUSTRIAL DE SANTANDER   (Colombia)

^b CSIC   (Spain)

Author keywords

CALB; Chemical modification; Enzyme distribution on the support; Enzyme hyperactivation; Enzyme stabilization; Glutaraldehyde; Octyl agarose

Indexed keywords

AGAROSE; AMINO GROUP; CALB; ENZYME MODIFICATION; ENZYME MOLECULES; ENZYME STABILIZATION; GLUTARALDEHYDE CROSS-LINKING; GLUTARALDEHYDES; IMMOBILIZATION RATES; INTERMOLECULAR BONDS; INTERMOLECULAR CROSSLINKING; LARGE AGGREGATES; LIPASE B FROM CANDIDA ANTARCTICA; MODIFICATION DEGREES; MOLECULAR MODIFICATION; SDS-PAGE; SODIUM PHOSPHATE; THERMAL INACTIVATION;

ALDEHYDES; BIOCATALYSTS; CHEMICAL MODIFICATION; CROSSLINKING; DESORPTION; ETHANOL; EXPERIMENTS; SODIUM COMPOUNDS; STABILIZATION;

ENZYME IMMOBILIZATION;

CANDIDA ANTARCTICA;

EID: 84859431657     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2012.02.009     Document Type: Article

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