Generation of soluble and active subtilisin and alpha-chymotrypsin in organic solvents via hydrophobic ion pairing.
Int J Pept Protein Res
; 47(3): 177-81, 1996 Mar.
Article
em En
| MEDLINE
| ID: mdl-8740967
ABSTRACT
With very low concentrations of anionic detergents, such as sodium dodecyl sulfate (SDS) and Aerosol OT (AOT), it is possible to solubilize proteases in organic solvents, while retaining enzymatic activity. For example, the SDS-subtilisin BPN' complex catalyzes transesterification of Ac-Phe-OMe in ethanol with a kcat/Km of 36 M-1 s-1 for mutant M1 and 39 M-1 s-1 for the wild type. By comparison, M1 suspended in ethanol is approximately 1000-fold less active, with a kcat/Km of 0.03 M-1 s-1. Similarly, AOT complexes of alpha-chymotrypsin were found to be approximately 1000 times more active (kcat/Km = 100-350 M-1 s-1) than the suspended enzyme.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Quimotripsina
/
Subtilisinas
Idioma:
En
Revista:
Int J Pept Protein Res
Ano de publicação:
1996
Tipo de documento:
Article
País de afiliação:
Estados Unidos