A kinetic model for enzyme interfacial activity and stability: pa-hydroxynitrile lyase at the diisopropyl ether/water interface

Biotechnology and Bioengineering

Volumn 78, Issue 6, 2002, Pages 595-605

  Cascão Pereira, Luis G ^a   Hickel, Andrea ^b   Radke, Clayton J ^a   Blanch, Harvey W ^a  

^a University of California   (United States)

^b ERICH SCHMID INSTITUTE OF MATERIALS SCIENCE   (Austria)

Author keywords

Dynamic tension lag time; Hydroxynitrile lyase; Interfacial enzyme catalysis; Kinetic model; Two phase systems

Indexed keywords

ADSORPTION; ALDEHYDES; BENZENE; ENZYME KINETICS; SURFACE TENSION;

ENZYME ACTIVITY;

BIOTECHNOLOGY;

BENZALDEHYDE; HYDROXYNITRILE LYASE;

ADSORPTION; AQUEOUS SOLUTION; ARTICLE; CATALYSIS; CHEMICAL REACTION KINETICS; CONFORMATIONAL TRANSITION; ENANTIOMER; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME STABILITY; LIQUID LIQUID EXTRACTION; PROTEIN DENATURATION; PROTEIN TRANSPORT;

ADSORPTION; ALDEHYDE-LYASES; CATALYSIS; ENZYME STABILITY; ETHERS; KINETICS; MODELS, CHEMICAL; PRUNUS; SOLVENTS; TIME; WATER;

PRUNUS; PRUNUS DULCIS;

EID: 0037142394     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.10241     Document Type: Article

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