Biotechnology Letters

, 31:101

Purification and some properties of an extracellular ribonuclease with antiviral activity against tobacco mosaic virus from Bacillus cereus

Original Research Paper

DOI: 10.1007/s10529-008-9831-1

Cite this article as:
Zhou, WW. & Niu, TG. Biotechnol Lett (2009) 31: 101. doi:10.1007/s10529-008-9831-1


A new ribonuclease (RNase) with tobacco mosaic virus inhibition was isolated and purified from Bacillus cereus ZH14 through ammonium sulfate precipitation, ultrafiltration, ion-exchange chromatography of DEAE-Sephadex A-50 column, and gel chromatography of Sephacryl S-200HR column. The enzyme was purified approximately 134-fold with a recovery of 9.2%. The RNase had an MW of 75.6 kDa in SDS-PAGE, which differed from RNases reported previously. The inhibitory activity of the RNase in the purification process against tobacco mosaic virus was tested, and the percentage inhibition of the purified RNase (48 U/ml) reached 90%. The protein could tolerate 90°C and pH 4.0.


Antiviral protein Bacillus cereus Purification Ribonuclease Tobacco mosaic virus 

Copyright information

© Springer Science+Business Media B.V. 2008

Authors and Affiliations

  1. 1.College of Food Science and Nutritional EngineeringChina Agricultural UniversityBeijingChina

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