Literature DB >> 26433394

Microbial ribonucleases (RNases): production and application potential.

E Esin Hameş1, Tuğçe Demir2.   

Abstract

Ribonuclease (RNase) is hydrolytic enzyme that catalyzes the cleavage of phosphodiester bonds in RNA. RNases play an important role in the metabolism of cellular RNAs, such as mRNA and rRNA or tRNA maturation. Besides their cellular roles, RNases possess biological activity, cell stimulating properties, cytotoxicity and genotoxicity. Cytotoxic effect of particular microbial RNases was comparable to that of animal derived counterparts. In this respect, microbial RNases have a therapeutic potential as anti-tumor drugs. The significant development of DNA vaccines and the progress of gene therapy trials increased the need for RNases in downstream processes. In addition, RNases are used in different fields, such as food industry for single cell protein preparations, and in some molecular biological studies for the synthesis of specific nucleotides, identifying RNA metabolism and the relationship between protein structure and function. In some cases, the use of bovine or other animal-derived RNases have increased the difficulties due to the safety and regulatory issues. Microbial RNases have promising potential mainly for pharmaceutical purposes as well as downstream processing. Therefore, an effort has been given to determination of optimum fermentation conditions to maximize RNase production from different bacterial and fungal producers. Also immobilization or strain development experiments have been carried out.

Entities:  

Keywords:  Antitumor; Downstream process; Microbial RNase; Optimization; Production; Ribonuclease (RNase)

Mesh:

Substances:

Year:  2015        PMID: 26433394     DOI: 10.1007/s11274-015-1945-8

Source DB:  PubMed          Journal:  World J Microbiol Biotechnol        ISSN: 0959-3993            Impact factor:   3.312


  82 in total

1.  Purification, crystallization and preliminary X-ray analysis of two crystal forms of ribonuclease Sa3.

Authors:  V Hlinková; L Urbániková; D Krajcíková; J Sevcík
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2001-04-24

2.  The Sso7d DNA-binding protein from Sulfolobus solfataricus has ribonuclease activity.

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Journal:  FEBS Lett       Date:  2001-05-25       Impact factor: 4.124

3.  Bacillus intermedius ribonuclease as inhibitor of cell proliferation and membrane current.

Authors:  O Ilinskaya; K Decker; A Koschinski; F Dreyer; H Repp
Journal:  Toxicology       Date:  2001-01-02       Impact factor: 4.221

Review 4.  Recent insights into the structure and function of the ribonucleoprotein enzyme ribonuclease P.

Authors:  Michael E Harris; Eric L Christian
Journal:  Curr Opin Struct Biol       Date:  2003-06       Impact factor: 6.809

Review 5.  RNase A ribonucleases and host defense: an evolving story.

Authors:  Helene F Rosenberg
Journal:  J Leukoc Biol       Date:  2008-01-22       Impact factor: 4.962

6.  Optimization of fermentation conditions for production of anti-TMV extracellular ribonuclease by Bacillus cereus using response surface methodology.

Authors:  Wen-Wen Zhou; Yun-Long He; Tian-Gui Niu; Jian-Jiang Zhong
Journal:  Bioprocess Biosyst Eng       Date:  2009-05-23       Impact factor: 3.210

7.  Studies on extracellular ribonucleases of Ustilago sphaerogena. Purification and properties.

Authors:  T Arima; T Uchida; F Egami
Journal:  Biochem J       Date:  1968-02       Impact factor: 3.857

8.  tRNA maturation in Aquifex aeolicus.

Authors:  Dagmar K Willkomm; Ralph Feltens; Roland K Hartmann
Journal:  Biochimie       Date:  2002-08       Impact factor: 4.079

9.  Guanyl-specific ribonuclease from the fungus Penicillium chrysogenum strain 152 and its complex with guanosine 3'-phosphate studied by nuclear magnetic resonance.

Authors:  G I Yakovlev; M Y Karpeisky; S I Bezborodova; O P Beletskaja; V G Sakharovsky
Journal:  Eur J Biochem       Date:  1980-08

10.  Regulation of a Neurospora crassa extracellular RNase by phosphorus, nitrogen, and carbon derepressions.

Authors:  R A Lindberg; H Drucker
Journal:  J Bacteriol       Date:  1984-02       Impact factor: 3.490

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