Ricerca avanzata

Home > Riviste > Minerva Biotecnologica > Fascicoli precedenti > Minerva Biotecnologica 2013 Settembre;25(3) > Minerva Biotecnologica 2013 Settembre;25(3):165-70



Rivista di Biologia Molecolare e Biotecnologie

Indexed/Abstracted in: EMBASE, Science Citation Index Expanded (SciSearch), Scopus
Impact Factor 0,246

Periodicità: Trimestrale

ISSN 1120-4826

Online ISSN 1827-160X


Minerva Biotecnologica 2013 Settembre;25(3):165-70


Production, purification and biochemical analysis of RNase producing mutant strain of Streptomyces venezuelae

Sunhare R. 1, 2, Punniyamoorthy G. 3, Prabu R. 2, 4

1 Institute of Bioscience, Universiti Putra Malaysia, UPM Serdang, Selangor, Malaysia;
2 School of Biotechnology, University Institute of Technology, Rajiv Gandhi Proudyogiki Vishiwavidyalaya, Bhopal, India;
3 Department of Biochemistry, M.R Government College, Mannargudi, India;
4 Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, UPM Serdang, Selangor, Malaysia

Aim: The aim of this study was to improve the intracellular and extracellular RNase producing Streptomyces venezuelae strain.
Methods: The random mutation was subjected into Streptomyces venezuelae with N-Methyl-N’ nitro-N-nitrosoguanidine (NTG) to increase the RNase enzyme production. The presence of the enzyme was confirmed by RNase activity method and Native-PAGE electrophoresis. This RNase R family was purified by multistep purifications with cation-exchange chromatography and size exclusive chromatography respectively.
Results: There was 3-4fold increment in RNase R enzyme has observed with selected N-Methyl-N’ nitoro-N-nitrosognanidine (NTG) mutated clones. The purified RNase shows stability against various metal ions with enzyme activity at pH 7 and temperature 37°C.
Conclusion: These approaches are able to resolve the contradiction between the low production and high demand of RNase enzyme.

lingua: Inglese


inizio pagina