Screening and molecular characterization of Serratia marcescens VITSD2: A strain producing optimum serratiopeptidase

Abstract

The current work was attempted to isolate and characterize the serratiopeptidase producing Serratia sp. Among the 10 bacterial isolates 7 strains were identified as Serratia sp. Out of 7 strains one showed potent proteolytic activity and selected for further studies. Based on the morphological, biochemical and molecular characterization, the potent isolate (RH03) was identified as Serratia marcescens (GenBank accession number: KC961637) and the strain was designated as Serratia marcescens VITSD2. The production of serratiopeptidase was carried out in trypticase soya broth and the enzyme was partially purified using ammonium sulfate precipitation and dialysis. The specific activity was determined by casein hydrolysis assay and was found to be 12.00, 21.33, and 25.40 units/mg for crude, precipitated and dialysed samples. The molecular weight of the protease was determined by SDS-PAGE and it was found to be 50 kDa. The antibacterial activity of the produced serratiopeptidase showed moderate activity against Pseudomonas aeruginosa MTCC No. 4676 (12 mm) and Escherichia coli MTCC No. 1588 (15 mm).

Keywords

Serratiopeptidase / Serratia marcescens VITSD2 / antibacterial activity

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Acknowledegment

We are greatly indebted to Vellore Institute of Technology for the constant encouragement, help and support for extending necessary facilities.

Conflict of interest

Subathra, Renuka, Harini, Jemimah and Mohanasrinivasan declare that they have no conflict of interest.

This article does not contain any studies with human or animal subjects performed by the any of the authors.

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2014 Higher Education Press and Springer-Verlag Berlin Heidelberg