Enhanced activity and stability of L-arabinose isomerase by immobilization on aminopropyl glass

Applied Microbiology and Biotechnology

Volumn 89, Issue 5, 2011, Pages 1435-1442

  Zhang, Ye Wang ^a,b   Jeya, Marimuthu ^a   Lee, Jung Kul ^a  

^a Konkuk University   (South Korea)

^b JIANGSU UNIVERSITY   (China)

Author keywords

Aminopropyl glass; Immobilization; L Arabinose isomerase; Stability

Indexed keywords

ADSORPTION CAPACITIES; AMINO GROUP; AMINOPROPYL; AMINOPROPYL GLASS; BACILLUS LICHENIFORMIS; BEFORE AND AFTER; CATALYTIC EFFICIENCIES; FREE ENZYME; GLUTARALDEHYDES; IMMOBILIZATION; IMMOBILIZED ENZYME; L-ARABINOSE ISOMERASE; PROTEIN G; REDUCING PARTICLE; RESPONSE SURFACE METHODOLOGY; THERMAL STABILITY;

ADSORPTION; ALDEHYDES; BACTERIOLOGY; ENZYME ACTIVITY; ENZYMES; GLASS; OPTIMIZATION; STABILITY;

ENZYME IMMOBILIZATION;

AMINOPROPYL GLASS; ARABINOSE; BACILLUS LICHENIFORMIS ARABINOSE ISOMERASE; BACTERIAL ENZYME; CELL ENZYME; GLASS IONOMER; UNCLASSIFIED DRUG;

ADSORPTION; BACTERIUM; ENZYME ACTIVITY; IMMOBILIZATION; PARTICLE SIZE; PH;

ARTICLE; BACILLUS LICHENIFORMIS; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME IMMOBILIZATION; ENZYME KINETICS; ENZYME STABILITY; INTERMETHOD COMPARISON; NONHUMAN; PARTICLE SIZE; PH; RESPONSE SURFACE METHOD; ROOM TEMPERATURE; THERMOSTABILITY;

ALDOSE-KETOSE ISOMERASES; BACILLUS; ENZYME STABILITY; ENZYMES, IMMOBILIZED; HYDROGEN-ION CONCENTRATION; KINETICS; SILICON DIOXIDE; TEMPERATURE;

BACILLUS LICHENIFORMIS;

EID: 79952574164     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-010-2966-8     Document Type: Article

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