, Volume 71, Issue 5, pp 563-570

Psychrophilic trypsin-type protease from Serratia proteamaculans

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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.

Original Russian Text © A. G. Mikhailova, V. V. Likhareva, R. F. Khairullin, N. L. Lubenets, L. D. Rumsh, I. V. Demidyuk, S. V. Kostrov, 2006, published in Biokhimiya, 2006, Vol. 71, No. 5, pp. 697–706.