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

ULTIMO FASCICOLO
 

JOURNAL TOOLS

eTOC
Per abbonarsi
Sottometti un articolo
Segnala alla tua biblioteca
 

ARTICLE TOOLS

Estratti
Permessi

 

ORIGINAL ARTICLES   

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

Copyright © 2013 EDIZIONI MINERVA MEDICA

lingua: Inglese

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


PDF


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.

inizio pagina