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Int. J. Mol. Sci. 2014, 15(1), 944-957; doi:10.3390/ijms15010944

Purification and Characterization of Iso-Ribonucleases from a Novel Thermophilic Fungus

Department of Food Science, Massachusetts Agricultural Experiment Station, University of Massachusetts, Amherst, MA 01003, USA
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Received: 10 December 2013 / Revised: 31 December 2013 / Accepted: 2 January 2014 / Published: 10 January 2014
(This article belongs to the Special Issue Thermophilic DNases, RNases and Proteases)
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Abstract

A thermophilic fungus previously isolated from composted horse manure was found to produce extracellular iso-RNases that were purified 127.6-fold using a combination of size exclusion chromatography and a novel affinity membrane purification system. The extent of purification was determined electrophoretically using 4%–15% gradient polyacrylamide gels. RNase activity was dependent on the presence of a metal co-factor with significantly more activity with Zn2+ or Mn2+ than Mg2+. The RNases exhibited maximum activity at both pH 3.0 and pH 7.0 with no activity at pH 2.0 or 10.0. The optimal temperature for the iso-RNase was 70 °C. The molecular weight of the iso-RNase was determined to be 69 kDa using a Sephadex G-75 column.
Keywords: affinity purification; RNase purification; chromatography; thermophilic fungi; RNase characterization affinity purification; RNase purification; chromatography; thermophilic fungi; RNase characterization
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Landry, K.S.; Levin, R.E. Purification and Characterization of Iso-Ribonucleases from a Novel Thermophilic Fungus. Int. J. Mol. Sci. 2014, 15, 944-957.

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