Article

Biochemistry (Moscow)

, Volume 71, Issue 5, pp 563-570

First online:

Psychrophilic trypsin-type protease from Serratia proteamaculans

  • A. G. MikhailovaAffiliated withShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences Email author 
  • , V. V. LikharevaAffiliated withShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
  • , R. F. KhairullinAffiliated withShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
  • , N. L. LubenetsAffiliated withShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
  • , L. D. RumshAffiliated withShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
  • , I. V. DemidyukAffiliated withInstitute of Molecular Genetics, Russian Academy of Sciences
  • , S. V. KostrovAffiliated withInstitute of Molecular Genetics, Russian Academy of Sciences

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Abstract

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.

Key words

psychrophilic enzymes trypsin Serratia proteamaculans affinity chromatography substrate-inhibitor analysis