Screening, purification and characterization of the thermoalkalophilic lipase produced by Bacillus thermoleovorans CCR11
Among eleven aerobic thermophilic Bacillus strains, isolated from “El Carrizal” hot springs in Veracruz, Mexico, Bacillus thermoleovorans CCR11 (EMBL # AJ536599) was selected for lipase characterization because of its high lipase specific activity. Lipase was purified by diafiltration (polyethersulf...
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| Veröffentlicht in: | Enzyme and microbial technology 2005-11, Vol.37 (6), p.648-654 |
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| creator | Castro-Ochoa, Lelie D. Rodríguez-Gómez, Citlali Valerio-Alfaro, Gerardo Oliart Ros, Rosamaría |
| description | Among eleven aerobic thermophilic
Bacillus strains, isolated from “El Carrizal” hot springs in Veracruz, Mexico,
Bacillus thermoleovorans CCR11 (EMBL # AJ536599) was selected for lipase characterization because of its high lipase specific activity. Lipase was purified by diafiltration (polyethersulfone ultrafiltration membrane co500,000), and preparative isoelectrofocusing. The lipase had a relative molecular mass of 11
kDa (the lowest
M
r reported), although it formed higher molecular weight aggregates in native form. The optimum catalytic conditions for
Bacillus thermoleovorans CCR11 lipase were 60
°C and pH 9–10. Hg
2+, PMSF, SDS, Tween 80 and Tween 20 had an inhibitory effect on lipase activity, whereas Ca
2+ salts and Triton X-100 increased it. Lipase activity was compatible with the presence of organic solvents, except for butanol. Lipase showed a notable preference for C6–C10
p-nitrophenyl esters, with the highest activity toward
p-nitrophenyl caproate (C10). Lipase stability in the presence of organic solvents, as well as in acidic and alkaline pHs and at high temperatures makes it a good candidate for its application in non-aqueous biocatalysis. |
| doi_str_mv | 10.1016/j.enzmictec.2005.06.003 |
| format | Article |
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Bacillus strains, isolated from “El Carrizal” hot springs in Veracruz, Mexico,
Bacillus thermoleovorans CCR11 (EMBL # AJ536599) was selected for lipase characterization because of its high lipase specific activity. Lipase was purified by diafiltration (polyethersulfone ultrafiltration membrane co500,000), and preparative isoelectrofocusing. The lipase had a relative molecular mass of 11
kDa (the lowest
M
r reported), although it formed higher molecular weight aggregates in native form. The optimum catalytic conditions for
Bacillus thermoleovorans CCR11 lipase were 60
°C and pH 9–10. Hg
2+, PMSF, SDS, Tween 80 and Tween 20 had an inhibitory effect on lipase activity, whereas Ca
2+ salts and Triton X-100 increased it. Lipase activity was compatible with the presence of organic solvents, except for butanol. Lipase showed a notable preference for C6–C10
p-nitrophenyl esters, with the highest activity toward
p-nitrophenyl caproate (C10). Lipase stability in the presence of organic solvents, as well as in acidic and alkaline pHs and at high temperatures makes it a good candidate for its application in non-aqueous biocatalysis.</description><identifier>ISSN: 0141-0229</identifier><identifier>EISSN: 1879-0909</identifier><identifier>DOI: 10.1016/j.enzmictec.2005.06.003</identifier><identifier>CODEN: EMTED2</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>Bacillus thermoleovorans ; Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; Enzyme characterization ; Fundamental and applied biological sciences. Psychology ; Lipase ; Miscellaneous ; Mission oriented research ; Thermophile</subject><ispartof>Enzyme and microbial technology, 2005-11, Vol.37 (6), p.648-654</ispartof><rights>2005 Elsevier Inc.</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c442t-45d9d53c5edb81a96d99b7487fc3744f0ee52092f920cb7f7757d6ff097ea5743</citedby><cites>FETCH-LOGICAL-c442t-45d9d53c5edb81a96d99b7487fc3744f0ee52092f920cb7f7757d6ff097ea5743</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.enzmictec.2005.06.003$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17123673$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Castro-Ochoa, Lelie D.</creatorcontrib><creatorcontrib>Rodríguez-Gómez, Citlali</creatorcontrib><creatorcontrib>Valerio-Alfaro, Gerardo</creatorcontrib><creatorcontrib>Oliart Ros, Rosamaría</creatorcontrib><title>Screening, purification and characterization of the thermoalkalophilic lipase produced by Bacillus thermoleovorans CCR11</title><title>Enzyme and microbial technology</title><description>Among eleven aerobic thermophilic
Bacillus strains, isolated from “El Carrizal” hot springs in Veracruz, Mexico,
Bacillus thermoleovorans CCR11 (EMBL # AJ536599) was selected for lipase characterization because of its high lipase specific activity. Lipase was purified by diafiltration (polyethersulfone ultrafiltration membrane co500,000), and preparative isoelectrofocusing. The lipase had a relative molecular mass of 11
kDa (the lowest
M
r reported), although it formed higher molecular weight aggregates in native form. The optimum catalytic conditions for
Bacillus thermoleovorans CCR11 lipase were 60
°C and pH 9–10. Hg
2+, PMSF, SDS, Tween 80 and Tween 20 had an inhibitory effect on lipase activity, whereas Ca
2+ salts and Triton X-100 increased it. Lipase activity was compatible with the presence of organic solvents, except for butanol. Lipase showed a notable preference for C6–C10
p-nitrophenyl esters, with the highest activity toward
p-nitrophenyl caproate (C10). Lipase stability in the presence of organic solvents, as well as in acidic and alkaline pHs and at high temperatures makes it a good candidate for its application in non-aqueous biocatalysis.</description><subject>Bacillus thermoleovorans</subject><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>Enzyme characterization</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Lipase</subject><subject>Miscellaneous</subject><subject>Mission oriented research</subject><subject>Thermophile</subject><issn>0141-0229</issn><issn>1879-0909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqFkEtvEzEQgC0EEqHwG_AFTuwy9nrX8bFE5SFVqtSWs-XYY-LgrBd7t6L99ThKBEcOo5FG37w-Qt4yaBmw4eO-xfHpEOyMtuUAfQtDC9A9Iyu2lqoBBeo5WQETrAHO1UvyqpQ9QC0IWJHfdzYjjmH88YFOSw4-WDOHNFIzOmp3Jps6OIenUzF5Ou_wGPmQTPxpYpp2IQZLY5hMQTrl5BaLjm4f6SdjQ4xLOeMR00PKZix0s7ll7DV54U0s-OacL8j3z1f3m6_N9c2Xb5vL68YKwedG9E65vrM9uu2aGTU4pbZSrKW3nRTCA2LPQXGvONit9FL20g3eg5Joeim6C_L-NLee9mvBMutDKBZjNCOmpWgmoVcdHyooT6DNqZSMXk85HEx-1Az00bTe67-m9dG0hkFX07Xz3XmFKdZEX5-0ofxrl4x3gzxylycO678PAbMuNuBYdYWMdtYuhf_u-gP0jZsn</recordid><startdate>20051101</startdate><enddate>20051101</enddate><creator>Castro-Ochoa, Lelie D.</creator><creator>Rodríguez-Gómez, Citlali</creator><creator>Valerio-Alfaro, Gerardo</creator><creator>Oliart Ros, Rosamaría</creator><general>Elsevier Inc</general><general>Elsevier Science</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20051101</creationdate><title>Screening, purification and characterization of the thermoalkalophilic lipase produced by Bacillus thermoleovorans CCR11</title><author>Castro-Ochoa, Lelie D. ; Rodríguez-Gómez, Citlali ; Valerio-Alfaro, Gerardo ; Oliart Ros, Rosamaría</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c442t-45d9d53c5edb81a96d99b7487fc3744f0ee52092f920cb7f7757d6ff097ea5743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Bacillus thermoleovorans</topic><topic>Biological and medical sciences</topic><topic>Biology of microorganisms of confirmed or potential industrial interest</topic><topic>Biotechnology</topic><topic>Enzyme characterization</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Lipase</topic><topic>Miscellaneous</topic><topic>Mission oriented research</topic><topic>Thermophile</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Castro-Ochoa, Lelie D.</creatorcontrib><creatorcontrib>Rodríguez-Gómez, Citlali</creatorcontrib><creatorcontrib>Valerio-Alfaro, Gerardo</creatorcontrib><creatorcontrib>Oliart Ros, Rosamaría</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Enzyme and microbial technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Castro-Ochoa, Lelie D.</au><au>Rodríguez-Gómez, Citlali</au><au>Valerio-Alfaro, Gerardo</au><au>Oliart Ros, Rosamaría</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Screening, purification and characterization of the thermoalkalophilic lipase produced by Bacillus thermoleovorans CCR11</atitle><jtitle>Enzyme and microbial technology</jtitle><date>2005-11-01</date><risdate>2005</risdate><volume>37</volume><issue>6</issue><spage>648</spage><epage>654</epage><pages>648-654</pages><issn>0141-0229</issn><eissn>1879-0909</eissn><coden>EMTED2</coden><abstract>Among eleven aerobic thermophilic
Bacillus strains, isolated from “El Carrizal” hot springs in Veracruz, Mexico,
Bacillus thermoleovorans CCR11 (EMBL # AJ536599) was selected for lipase characterization because of its high lipase specific activity. Lipase was purified by diafiltration (polyethersulfone ultrafiltration membrane co500,000), and preparative isoelectrofocusing. The lipase had a relative molecular mass of 11
kDa (the lowest
M
r reported), although it formed higher molecular weight aggregates in native form. The optimum catalytic conditions for
Bacillus thermoleovorans CCR11 lipase were 60
°C and pH 9–10. Hg
2+, PMSF, SDS, Tween 80 and Tween 20 had an inhibitory effect on lipase activity, whereas Ca
2+ salts and Triton X-100 increased it. Lipase activity was compatible with the presence of organic solvents, except for butanol. Lipase showed a notable preference for C6–C10
p-nitrophenyl esters, with the highest activity toward
p-nitrophenyl caproate (C10). Lipase stability in the presence of organic solvents, as well as in acidic and alkaline pHs and at high temperatures makes it a good candidate for its application in non-aqueous biocatalysis.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><doi>10.1016/j.enzmictec.2005.06.003</doi><tpages>7</tpages></addata></record> |
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| source | Elsevier ScienceDirect Journals |
| subjects | Bacillus thermoleovorans Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Enzyme characterization Fundamental and applied biological sciences. Psychology Lipase Miscellaneous Mission oriented research Thermophile |
| title | Screening, purification and characterization of the thermoalkalophilic lipase produced by Bacillus thermoleovorans CCR11 |
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