RT - Journal Article T1 - Molecular Screening of Serratia Marcescens Producing Serratiopeptidase Enzyme and Prodigiosin Pigment from Paddy Field Waters in West Mazandaran JF - NCMBJ YR - 2015 JO - NCMBJ VO - 5 IS - 18 UR - http://ncmbjpiau.ir/article-1-628-en.html SP - 55 EP - 62 K1 - Serratia marcescens K1 - 16SrRNA K1 - Serratiopeptidase K1 - Prodigiosin K1 - spectrophotometry AB - Aims and Background: Serratiopeptidase is a proteolyitic enzyme produced from Serratia Sp. and is used as a medicine against chronic inflammatory diseases. Prodigiosin is also produced by Serratia marcescens and is used in medicine production. This paper aims to separate and discover a novel strain (which is able to produce Serratiopeptidase and Prodigiosin) of Serratia marcescens from paddy field waters located in western Mazandaran. Materials and Methods: In this study, 50 water samples were collected under standard conditions from paddy fields. As many as 40 bacteria samples were separated among which 10 bacteria samples had protease activity and Prodigiosin. They were separated using biochemical tests. Then, the strain was discovered using 16SrRNA. The molecular weight of the enzyme was measured using protein deposition and SDS-PAGE. Then, Prodigiosin production capability was experimented using ultraviolet spectrophotometry at wavelength 535 nm under 25, 28, and 37 0C in the following culturing environments: nutrient broth, MacConkey broth, Luria-Bertani Broth, and skim milk agar. Results: Only one isolate was discovered. Its molecular weight was about 52 kda. Pigment production was maximized in skim milk agar at 28 0C. The bacteria were able to produce the pigment even at 37 0C. Conclusion: Considering the importance of Serratiopeptidase and Prodigiosin, we recommend to optimize the conditions to produce them in a larger amount. The molecular weight of Serratiopeptidase was 52 kda. This result confirms the observations of Mohankumar et. al. 2011. Pigment production was entirely stopped under 37˚C. This result confirms the observations of Pryce and Terry 2000. LA eng UL http://ncmbjpiau.ir/article-1-628-en.html M3 ER -