<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ArticleSet PUBLIC "-//NLM//DTD PubMed 2.7//EN" "https://dtd.nlm.nih.gov/ncbi/pubmed/in/PubMed.dtd">
<ArticleSet>
<Article>
<Journal>
				<PublisherName>University of Tehran</PublisherName>
				<JournalTitle>Journal of Sciences, Islamic Republic of Iran</JournalTitle>
				<Issn>1016-1104</Issn>
				<Volume>23</Volume>
				<Issue>1</Issue>
				<PubDate PubStatus="epublish">
					<Year>2012</Year>
					<Month>03</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>Isolation, Purification and Characterization of a Thermophilic Alkaline Protease from 
Bacillus subtilis BP-36</ArticleTitle>
<VernacularTitle>Isolation, Purification and Characterization of a Thermophilic Alkaline Protease from 
Bacillus subtilis BP-36</VernacularTitle>
			<FirstPage>7</FirstPage>
			<LastPage>13</LastPage>
			<ELocationID EIdType="pii">24564</ELocationID>
			
			
			<Language>EN</Language>
<AuthorList>
<Author>
					<FirstName>E.</FirstName>
					<LastName>Omidinia</LastName>
<Affiliation>Pasteur Institute of Iran</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>1970</Year>
					<Month>01</Month>
					<Day>01</Day>
				</PubDate>
			</History>
		<Abstract>The goal of this research was to isolate and identify the thermostable alkaline protease producing bacteria among several native Iranian microorganisms. At the end of screening program, a Bacillus subtilis BP-36 strain producing thermophilic alkaline protease was isolated from a hot spring in Ardebil province. The target enzyme was purified using a one-step Aqueous two-phase systems (ATPS) protocol involving 22% (w/w) polyethylene glycol (PEG)-10,000, and 18% (w/w) citrate with a yield of 39.7%, specific activity of 2600 U/mg and purification factor of 4.8. It was shown to have a molecular weight of 40 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The purified thermophile enzyme was stable in alkaline pH range (9.0-11.0) with the optimum pH of 9.0. It was highly stable at 60 °C and retained 100% activity even after 90 minutes, suggesting that it belong to the family of thermophilous. Collectively, our obtained data revealed that the thermophilic protease produced by B. subtilis BP-36 has the potential application in industrial processes under high temperature.</Abstract>
		<ObjectList>
			<Object Type="keyword">
			<Param Name="value">Alkaline protease</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">Thermophilic</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">Bacillus subtilis</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">isolation</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">purification</Param>
			</Object>
		</ObjectList>
<ArchiveCopySource DocType="pdf">https://jsciences.ut.ac.ir/article_24564_f333f1e885ab0cd75ddacdd401d092d9.pdf</ArchiveCopySource>
</Article>
</ArticleSet>
