Psychrophilic trypsin-type protease from Serratia proteamaculans

• Published in: Biochemistry (Moscow) Vol. 71; no. 5; pp. 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: Journal Article
• Language: English
• Published: United States Springer 01.05.2006; Springer Nature B.V
• 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; Russia
• ISSN: 0006-2979; 1608-3040; 0320-9725
• DOI: 10.1134/S0006297906050166

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.