Psychrophilic Trypsin-Type Protease from Serratia proteamaculans

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A. G. Mikhailova^1*, V. V. Likhareva¹, R. F. Khairullin¹, N. L. Lubenets¹, L. D. Rumsh¹, I. V. Demidyuk², and S. V. Kostrov²

¹Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia; fax: (7-495) 335-7103; E-mail: anna@enzyme.siobc.ras.ru

²Institute of Molecular Genetics, Russian Academy of Sciences, pl. Akademika I. V. Kurchatova 2, 123182 Moscow, Russia; fax: (7-495) 196-0221; E-mail: duk@img.ras.ru

^* To whom correspondence should be addressed.

Received December 27, 2005; Revision received January 31, 2006

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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.

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Key words: psychrophilic enzymes, trypsin, Serratia proteamaculans, affinity chromatography, substrate-inhibitor analysis

DOI: 10.1134/S0006297906050166

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