Psychrophilic trypsin-type protease from Serratia proteamaculans

A preparative method for purification of a novel protease from the psychrotolerant Gram-negative microorganism Serratia proteamaculans (PSP) was developed using affinity chromatography on BPTI-Sepharose. It yielded electrophoretically homogeneous PSP preparation of 60 kD. The PSP properties (tempera...

Full description

Saved in:
Bibliographic Details
Published in:Biochemistry (Moscow) 2006-05, Vol.71 (5), p.563-570
Main Authors: Mikhailova, A G, Likhareva, V V, Khairullin, R F, Lubenets, N L, Rumsh, L D, Demidyuk, I V, Kostrov, S V
Format: Article
Language:English
Subjects:
Affinity chromatography
Bacteria
Bacterial Proteins - antagonists & inhibitors
Bacterial Proteins - isolation & purification
Bacterial Proteins - metabolism
Chromatography, Affinity - methods
Chromatography, Ion Exchange - methods
Enzyme Stability - drug effects
Enzymes
Hydrogen-Ion Concentration
Kinetics
Nocardia corallina
Peptide Hydrolases - isolation & purification
Peptide Hydrolases - metabolism
Protease
Protease Inhibitors - pharmacology
Proteinase
Psychrotrophic organisms
Serratia
Serratia - enzymology
Serratia proteamaculans
Substrate inhibition
Substrate Specificity
Temperature
Trypsin
Trypsin - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A preparative method for purification of a novel protease from the psychrotolerant Gram-negative microorganism Serratia proteamaculans (PSP) was developed using affinity chromatography on BPTI-Sepharose. It yielded electrophoretically homogeneous PSP preparation of 60 kD. The PSP properties (temperature and pH stability, high catalytic efficiency) indicate that this enzyme can be defined as a psychrophilic protease. Inhibitory analysis together with substrate specificity indicates that the studied PSP exhibits properties of serine trypsin-like and Zn-dependent protease.
ISSN:0006-2979
1608-3040
0320-9725
DOI:10.1134/S0006297906050166