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Biochemical characterization of an alkaline surfactant-stable keratinase from a new keratinase producer, Bacillus zhangzhouensis
A new keratinase producer, Bacillus sp. BK111, isolated from a poultry feather was identified as Bacillus zhangzhouensis , which is the first report for its keratinolytic activity. The keratinase production was optimized, followed by the enzyme purification and characterization using biochemical ass...
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| Published in: | Extremophiles : life under extreme conditions 2020-09, Vol.24 (5), p.693-704 |
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| cites | cdi_FETCH-LOGICAL-c352t-4a7e97fd6718a424063192543d2c7f5a8d408f9471293ae1e86d1bf41a86862a3 |
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| container_title | Extremophiles : life under extreme conditions |
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| creator | Moridshahi, Roghyeh Bahreini, Masoumeh Sharifmoghaddam, Mohammadreza Asoodeh, Ahmad |
| description | A new keratinase producer,
Bacillus
sp. BK111, isolated from a poultry feather was identified as
Bacillus zhangzhouensis
, which is the first report for its keratinolytic activity. The keratinase production was optimized, followed by the enzyme purification and characterization using biochemical assays. A 2.34-fold increase was observed in the enzyme production under optimized conditions. The enzyme was characterized as a serine protease with 42 kDa molecular weight, stable in a wide range of temperature and pH with maximum keratinolytic activity at 60 °C and pH 9.5. The enzyme had a wide range of different substrates with the best performance on the feather meal substrate. Metal ions of Ca
2+
, K
+
, Na
+
and Mn
2+
enhanced the enzyme activity. The enzyme showed a great deal of stability in the presence of ethanol, methanol, acetone, 2-propanol, dimethyl sulfoxide, Tween-80 and Triton X-100. Dithiothreitol (DTT), as a reducing agent, caused a twofold increase in keratinolytic activity. The half-life of the enzyme at optimum temperature was calculated to be 125 min and the ratio of keratinolytic:caseinolytic for the enzyme was 0.8. Our results showed the remarkable features of the enzyme that make it suitable for biotechnological usages. |
| doi_str_mv | 10.1007/s00792-020-01187-9 |
| format | article |
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Bacillus
sp. BK111, isolated from a poultry feather was identified as
Bacillus zhangzhouensis
, which is the first report for its keratinolytic activity. The keratinase production was optimized, followed by the enzyme purification and characterization using biochemical assays. A 2.34-fold increase was observed in the enzyme production under optimized conditions. The enzyme was characterized as a serine protease with 42 kDa molecular weight, stable in a wide range of temperature and pH with maximum keratinolytic activity at 60 °C and pH 9.5. The enzyme had a wide range of different substrates with the best performance on the feather meal substrate. Metal ions of Ca
2+
, K
+
, Na
+
and Mn
2+
enhanced the enzyme activity. The enzyme showed a great deal of stability in the presence of ethanol, methanol, acetone, 2-propanol, dimethyl sulfoxide, Tween-80 and Triton X-100. Dithiothreitol (DTT), as a reducing agent, caused a twofold increase in keratinolytic activity. The half-life of the enzyme at optimum temperature was calculated to be 125 min and the ratio of keratinolytic:caseinolytic for the enzyme was 0.8. Our results showed the remarkable features of the enzyme that make it suitable for biotechnological usages.</description><identifier>ISSN: 1431-0651</identifier><identifier>EISSN: 1433-4909</identifier><identifier>DOI: 10.1007/s00792-020-01187-9</identifier><language>eng</language><publisher>Tokyo: Springer Japan</publisher><subject>Acetone ; Bacillus zhangzhouensis ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; Calcium ; Calcium ions ; Dimethyl sulfoxide ; Dithiothreitol ; Enzymatic activity ; Enzyme activity ; Enzymes ; Ethanol ; Feathers ; Keratinase ; Keratinocytes ; Life Sciences ; Metal ions ; Metals ; Microbial Ecology ; Microbiology ; Molecular weight ; Original Paper ; pH effects ; Propanol ; Reducing agents ; Serine ; Serine proteinase ; Space life sciences ; Stability ; Substrates ; Temperature effects ; Water purification</subject><ispartof>Extremophiles : life under extreme conditions, 2020-09, Vol.24 (5), p.693-704</ispartof><rights>Springer Japan KK, part of Springer Nature 2020</rights><rights>Springer Japan KK, part of Springer Nature 2020.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c352t-4a7e97fd6718a424063192543d2c7f5a8d408f9471293ae1e86d1bf41a86862a3</citedby><cites>FETCH-LOGICAL-c352t-4a7e97fd6718a424063192543d2c7f5a8d408f9471293ae1e86d1bf41a86862a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27911,27912</link.rule.ids></links><search><creatorcontrib>Moridshahi, Roghyeh</creatorcontrib><creatorcontrib>Bahreini, Masoumeh</creatorcontrib><creatorcontrib>Sharifmoghaddam, Mohammadreza</creatorcontrib><creatorcontrib>Asoodeh, Ahmad</creatorcontrib><title>Biochemical characterization of an alkaline surfactant-stable keratinase from a new keratinase producer, Bacillus zhangzhouensis</title><title>Extremophiles : life under extreme conditions</title><addtitle>Extremophiles</addtitle><description>A new keratinase producer,
Bacillus
sp. BK111, isolated from a poultry feather was identified as
Bacillus zhangzhouensis
, which is the first report for its keratinolytic activity. The keratinase production was optimized, followed by the enzyme purification and characterization using biochemical assays. A 2.34-fold increase was observed in the enzyme production under optimized conditions. The enzyme was characterized as a serine protease with 42 kDa molecular weight, stable in a wide range of temperature and pH with maximum keratinolytic activity at 60 °C and pH 9.5. The enzyme had a wide range of different substrates with the best performance on the feather meal substrate. Metal ions of Ca
2+
, K
+
, Na
+
and Mn
2+
enhanced the enzyme activity. The enzyme showed a great deal of stability in the presence of ethanol, methanol, acetone, 2-propanol, dimethyl sulfoxide, Tween-80 and Triton X-100. Dithiothreitol (DTT), as a reducing agent, caused a twofold increase in keratinolytic activity. The half-life of the enzyme at optimum temperature was calculated to be 125 min and the ratio of keratinolytic:caseinolytic for the enzyme was 0.8. Our results showed the remarkable features of the enzyme that make it suitable for biotechnological usages.</description><subject>Acetone</subject><subject>Bacillus zhangzhouensis</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Calcium</subject><subject>Calcium ions</subject><subject>Dimethyl sulfoxide</subject><subject>Dithiothreitol</subject><subject>Enzymatic activity</subject><subject>Enzyme activity</subject><subject>Enzymes</subject><subject>Ethanol</subject><subject>Feathers</subject><subject>Keratinase</subject><subject>Keratinocytes</subject><subject>Life Sciences</subject><subject>Metal ions</subject><subject>Metals</subject><subject>Microbial Ecology</subject><subject>Microbiology</subject><subject>Molecular weight</subject><subject>Original Paper</subject><subject>pH effects</subject><subject>Propanol</subject><subject>Reducing agents</subject><subject>Serine</subject><subject>Serine proteinase</subject><subject>Space life sciences</subject><subject>Stability</subject><subject>Substrates</subject><subject>Temperature effects</subject><subject>Water purification</subject><issn>1431-0651</issn><issn>1433-4909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNp9kctOHTEMhkcVSOX2AqwidcOCtLlNZrIsqDcJiQ2sI5NxOIGchCYzQj0rHr2BUwnUBRvbsr_fsvx33TFnnzljw5faghGUCUYZ5-NAzYdujyspqTLM7LzUnDLd84_dfq13jPG-Dfa6p7OQ3QrXwUEkbgUF3IwlbGAOOZHsCSQC8R5iSEjqUnybQ5ppneEmIrnH0sgEFYkveU2AJHx8230oeVocllNyBi7EuFSyWUG63azygqmGetjteogVj_7lg-76-7er85_04vLHr_OvF9TJXsxUwYBm8JMe-AhKKKYlN6JXchJu8D2Mk2KjN2rgwkhAjqOe-I1XHEY9agHyoDvZ7m0X_V6wznYdqsMYIWFeqhVKtJ8o3g8N_fQfepeXktp1jZJam1Fp0yixpVzJtRb09qGENZQ_ljP7bIrdmmKbKfbFFPsskltRbXC6xfK6-h3VX4u8kMs</recordid><startdate>20200901</startdate><enddate>20200901</enddate><creator>Moridshahi, Roghyeh</creator><creator>Bahreini, Masoumeh</creator><creator>Sharifmoghaddam, Mohammadreza</creator><creator>Asoodeh, Ahmad</creator><general>Springer Japan</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H95</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L.G</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20200901</creationdate><title>Biochemical characterization of an alkaline surfactant-stable keratinase from a new keratinase producer, Bacillus zhangzhouensis</title><author>Moridshahi, Roghyeh ; Bahreini, Masoumeh ; Sharifmoghaddam, Mohammadreza ; Asoodeh, Ahmad</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c352t-4a7e97fd6718a424063192543d2c7f5a8d408f9471293ae1e86d1bf41a86862a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Acetone</topic><topic>Bacillus zhangzhouensis</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Calcium</topic><topic>Calcium ions</topic><topic>Dimethyl sulfoxide</topic><topic>Dithiothreitol</topic><topic>Enzymatic activity</topic><topic>Enzyme activity</topic><topic>Enzymes</topic><topic>Ethanol</topic><topic>Feathers</topic><topic>Keratinase</topic><topic>Keratinocytes</topic><topic>Life Sciences</topic><topic>Metal ions</topic><topic>Metals</topic><topic>Microbial Ecology</topic><topic>Microbiology</topic><topic>Molecular weight</topic><topic>Original Paper</topic><topic>pH effects</topic><topic>Propanol</topic><topic>Reducing agents</topic><topic>Serine</topic><topic>Serine proteinase</topic><topic>Space life sciences</topic><topic>Stability</topic><topic>Substrates</topic><topic>Temperature effects</topic><topic>Water purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moridshahi, Roghyeh</creatorcontrib><creatorcontrib>Bahreini, Masoumeh</creatorcontrib><creatorcontrib>Sharifmoghaddam, Mohammadreza</creatorcontrib><creatorcontrib>Asoodeh, Ahmad</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>ProQuest - 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Academic</collection><jtitle>Extremophiles : life under extreme conditions</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moridshahi, Roghyeh</au><au>Bahreini, Masoumeh</au><au>Sharifmoghaddam, Mohammadreza</au><au>Asoodeh, Ahmad</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biochemical characterization of an alkaline surfactant-stable keratinase from a new keratinase producer, Bacillus zhangzhouensis</atitle><jtitle>Extremophiles : life under extreme conditions</jtitle><stitle>Extremophiles</stitle><date>2020-09-01</date><risdate>2020</risdate><volume>24</volume><issue>5</issue><spage>693</spage><epage>704</epage><pages>693-704</pages><issn>1431-0651</issn><eissn>1433-4909</eissn><abstract>A new keratinase producer,
Bacillus
sp. BK111, isolated from a poultry feather was identified as
Bacillus zhangzhouensis
, which is the first report for its keratinolytic activity. The keratinase production was optimized, followed by the enzyme purification and characterization using biochemical assays. A 2.34-fold increase was observed in the enzyme production under optimized conditions. The enzyme was characterized as a serine protease with 42 kDa molecular weight, stable in a wide range of temperature and pH with maximum keratinolytic activity at 60 °C and pH 9.5. The enzyme had a wide range of different substrates with the best performance on the feather meal substrate. Metal ions of Ca
2+
, K
+
, Na
+
and Mn
2+
enhanced the enzyme activity. The enzyme showed a great deal of stability in the presence of ethanol, methanol, acetone, 2-propanol, dimethyl sulfoxide, Tween-80 and Triton X-100. Dithiothreitol (DTT), as a reducing agent, caused a twofold increase in keratinolytic activity. The half-life of the enzyme at optimum temperature was calculated to be 125 min and the ratio of keratinolytic:caseinolytic for the enzyme was 0.8. Our results showed the remarkable features of the enzyme that make it suitable for biotechnological usages.</abstract><cop>Tokyo</cop><pub>Springer Japan</pub><doi>10.1007/s00792-020-01187-9</doi><tpages>12</tpages></addata></record> |
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| identifier | ISSN: 1431-0651 |
| ispartof | Extremophiles : life under extreme conditions, 2020-09, Vol.24 (5), p.693-704 |
| issn | 1431-0651 1433-4909 |
| language | eng |
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| subjects | Acetone Bacillus zhangzhouensis Biochemistry Biomedical and Life Sciences Biotechnology Calcium Calcium ions Dimethyl sulfoxide Dithiothreitol Enzymatic activity Enzyme activity Enzymes Ethanol Feathers Keratinase Keratinocytes Life Sciences Metal ions Metals Microbial Ecology Microbiology Molecular weight Original Paper pH effects Propanol Reducing agents Serine Serine proteinase Space life sciences Stability Substrates Temperature effects Water purification |
| title | Biochemical characterization of an alkaline surfactant-stable keratinase from a new keratinase producer, Bacillus zhangzhouensis |
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