@article { ISI:000225723800036,
	title = {Extracellular nuclease from a thermophile, streptomyces thermonitrificans: production, purification and partial characterization of - double strand preferential - deoxyribonuclease activity},
	journal = {Process Biochemistry},
	volume = {40},
	number = {3-4},
	year = {2005},
	month = {MAR},
	pages = {1271-1278},
	publisher = {ELSEVIER SCI LTD},
	type = {Article},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND},
	abstract = {<p>A thermophilic strain of Streptomyces themionitrificans produced high levels of extracellular nuclease (designated as nuclease Stn beta) when grown on nutrient broth glucose medium. Maximal nuclease activity (51 U ml(-1)) was obtained, in 40 h, when the culture was grown on modified NBG medium at 45 degreesC. The enzyme was purified to homogeneity with an overall recovery of 5.6\% and a specific activity of 10,833. The relative molecular mass of the purified enzyme, determined by gel filtration, was 22.4 kDa and it showed an obligate requirement for Mn2+ for activity. The optimum pH and temperature of nuclease Stn beta were 8.0 and 45 degreesC, respectively. The enzyme was inhibited by Mg2+ CO2+, Cu2+, Zn2+ and Hg2+, inorganic phosphate, pyrophosphate, dithiothreitol, beta-mereaptoethanol, EDTA and NaCl. Nuclease Stn beta was stable to high concentrations of urea and organic solvents but susceptible to low concentrations of SDS and guanidine hydrochloride. Nuclease Stn beta is a multifunctional enzyme with substrate specificity in the order of dsDNA \&gt; ssDNA much greater than RNA. The end products of dsDNA hydrolysis were predominantly oligonucleotides (85-90\%) and small amounts of 5{\textquoteright} mononucleotides (10-15\%) suggesting an endo mode of action. (C) 2004 Elsevier Ltd. All rights reserved.</p>},
	keywords = {Characterization, Endonuclease, extracellular nuclease, production, Purification, Streptomyces thermonitrificans},
	issn = {1359-5113},
	doi = {10.1016/j.procbio.2004.05.015},
	author = {Patil, N. S. and Deshmukh, Satej S. and Shankar, V.}
}
@article { ISI:000292161300005,
	title = {Streptomyces nucleases},
	journal = {Critical Reviews in Microbiology},
	volume = {37},
	number = {3},
	year = {2011},
	month = {AUG},
	pages = {227-236},
	publisher = {INFORMA HEALTHCARE},
	address = {52 VANDERBILT AVE, NEW YORK, NY 10017 USA},
	abstract = {<p>Streptomyces nucleases are widely distributed and multifunctional enzymes acting on both DNA and RNA. They occur extra as well as intracellularly and can be classified under sugar specific and sugar non-specific nucleases. Nucleases play different roles like analytical, biological, and nutritional. They are also used in programmed cell death. Although more than 20 nucleases are reported to date, very little information is available regarding their structure-function relationship, active site based sequence homology, and the probable mechanism of action. This review describes the history, occurrence, localization, production, purification, properties, and applications of Streptomyces nucleases.</p>},
	keywords = {Applications, Endonuclease, extracellular, production, Purification, Substrate specificity},
	issn = {1040-841X},
	doi = {10.3109/1040841X.2011.562173},
	author = {Joshi, Amruta Pramod and Deshmukh, Sumedha Sharad}
}
