Production and Characterization of Organic Solvent-Tolerant Cellulase from Bacillus amyloliquefaciens AK9 Isolated from Hot Spring
A cellulase-producing bacterium, designated as strain AK9, was isolated from a hot spring of Tatta Pani, Azad Kashmir, Pakistan. The bacterium was identified as Bacillus amyloliquefaciens through 16S rRNA sequencing. Cellulase from strain AK9 was able to liberate glucose from soluble cellulose and c...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2017-08, Vol.182 (4), p.1390-1402 |
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| creator | Irfan, Muhammad Tayyab, Ammara Hasan, Fariha Khan, Samiullah Badshah, Malik Shah, Aamer Ali |
| description | A cellulase-producing bacterium, designated as strain AK9, was isolated from a hot spring of Tatta Pani, Azad Kashmir, Pakistan. The bacterium was identified as
Bacillus amyloliquefaciens
through 16S rRNA sequencing. Cellulase from strain AK9 was able to liberate glucose from soluble cellulose and carboxymethyl cellulose (CMC). Enzyme was purified through size exclusion chromatography and a single band of ∼47 kDa was observed on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme was purified with recovery of 35.5%, 3.6-fold purity with specific activity of 31 U mg
−1
. The purified cellulase retained its activity over a wide range of temperature (50–70 °C) and pH (3–7) with maximum stability at 60 °C and pH 5.0. The activity inhibited by ethylenediaminetetraacetic acid (EDTA), suggested that it was metalloenzyme. Diethyl pyrocarbonate (DEPC) and β-mercaptoethanol significantly inhibited cellulase activity that revealed the essentiality of histidine residues and disulfide bonds for its catalytic function. It was stable in non-ionic surfactants, in the presence of various metal ions, and in water-insoluble organic solvents. Approximately 9.1% of reducing sugar was released after enzymatic saccharification of DAP-pretreated agro-residue, compared to a very low percentage by autohydrolysis treatment. Hence, it is concluded that cellulase from
B. amyloliquefaciens
AK9 can potentially be used in bioconversion of lignocellulosic biomass to fermentable sugars. |
| doi_str_mv | 10.1007/s12010-017-2405-8 |
| format | Article |
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Bacillus amyloliquefaciens
through 16S rRNA sequencing. Cellulase from strain AK9 was able to liberate glucose from soluble cellulose and carboxymethyl cellulose (CMC). Enzyme was purified through size exclusion chromatography and a single band of ∼47 kDa was observed on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme was purified with recovery of 35.5%, 3.6-fold purity with specific activity of 31 U mg
−1
. The purified cellulase retained its activity over a wide range of temperature (50–70 °C) and pH (3–7) with maximum stability at 60 °C and pH 5.0. The activity inhibited by ethylenediaminetetraacetic acid (EDTA), suggested that it was metalloenzyme. Diethyl pyrocarbonate (DEPC) and β-mercaptoethanol significantly inhibited cellulase activity that revealed the essentiality of histidine residues and disulfide bonds for its catalytic function. It was stable in non-ionic surfactants, in the presence of various metal ions, and in water-insoluble organic solvents. Approximately 9.1% of reducing sugar was released after enzymatic saccharification of DAP-pretreated agro-residue, compared to a very low percentage by autohydrolysis treatment. Hence, it is concluded that cellulase from
B. amyloliquefaciens
AK9 can potentially be used in bioconversion of lignocellulosic biomass to fermentable sugars.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-017-2405-8</identifier><identifier>PMID: 28130767</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Bacillus amyloliquefaciens - growth & development ; Bacillus amyloliquefaciens - isolation & purification ; Bacillus amyloliquefaciens - metabolism ; Bacteria ; Biochemistry ; Bioconversion ; Biomass ; Biotechnology ; Carboxymethyl cellulose ; Carboxymethylcellulose ; Catalysis ; Cellulase ; Cellulase - biosynthesis ; Cellulase - isolation & purification ; Cellulase - metabolism ; Cellulose ; Chelating Agents - pharmacology ; Chemical bonds ; Chemistry ; Chemistry and Materials Science ; Culture Techniques ; Disulfide bonds ; Edetic acid ; Enzyme Stability - drug effects ; Enzymes ; Ethylenediaminetetraacetic acids ; Gel electrophoresis ; Glucose ; Histidine ; Hot springs ; Hot Springs - microbiology ; Hydrogen-Ion Concentration ; Hydrolysis ; Industry ; Ions ; Lignocellulose ; Lymphocytes B ; Metal ions ; Metals - pharmacology ; Organic chemicals ; Organic Chemicals - pharmacology ; Organic solvents ; Residues ; rRNA 16S ; Saccharification ; Size exclusion chromatography ; Sodium dodecyl sulfate ; Sodium lauryl sulfate ; Solvents ; Solvents - pharmacology ; Sugar ; Surface-Active Agents - pharmacology ; Surfactants ; Temperature ; Temperature effects</subject><ispartof>Applied biochemistry and biotechnology, 2017-08, Vol.182 (4), p.1390-1402</ispartof><rights>Springer Science+Business Media New York 2017</rights><rights>Applied Biochemistry and Biotechnology is a copyright of Springer, 2017.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-59c5090a62415e22542e1d691fb0f93c19e0f2af1173c0c4f375caf9cdd096fa3</citedby><cites>FETCH-LOGICAL-c409t-59c5090a62415e22542e1d691fb0f93c19e0f2af1173c0c4f375caf9cdd096fa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12010-017-2405-8$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-017-2405-8$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28130767$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Irfan, Muhammad</creatorcontrib><creatorcontrib>Tayyab, Ammara</creatorcontrib><creatorcontrib>Hasan, Fariha</creatorcontrib><creatorcontrib>Khan, Samiullah</creatorcontrib><creatorcontrib>Badshah, Malik</creatorcontrib><creatorcontrib>Shah, Aamer Ali</creatorcontrib><title>Production and Characterization of Organic Solvent-Tolerant Cellulase from Bacillus amyloliquefaciens AK9 Isolated from Hot Spring</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>A cellulase-producing bacterium, designated as strain AK9, was isolated from a hot spring of Tatta Pani, Azad Kashmir, Pakistan. The bacterium was identified as
Bacillus amyloliquefaciens
through 16S rRNA sequencing. Cellulase from strain AK9 was able to liberate glucose from soluble cellulose and carboxymethyl cellulose (CMC). Enzyme was purified through size exclusion chromatography and a single band of ∼47 kDa was observed on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme was purified with recovery of 35.5%, 3.6-fold purity with specific activity of 31 U mg
−1
. The purified cellulase retained its activity over a wide range of temperature (50–70 °C) and pH (3–7) with maximum stability at 60 °C and pH 5.0. The activity inhibited by ethylenediaminetetraacetic acid (EDTA), suggested that it was metalloenzyme. Diethyl pyrocarbonate (DEPC) and β-mercaptoethanol significantly inhibited cellulase activity that revealed the essentiality of histidine residues and disulfide bonds for its catalytic function. It was stable in non-ionic surfactants, in the presence of various metal ions, and in water-insoluble organic solvents. Approximately 9.1% of reducing sugar was released after enzymatic saccharification of DAP-pretreated agro-residue, compared to a very low percentage by autohydrolysis treatment. Hence, it is concluded that cellulase from
B. amyloliquefaciens
AK9 can potentially be used in bioconversion of lignocellulosic biomass to fermentable sugars.</description><subject>Bacillus amyloliquefaciens - growth & development</subject><subject>Bacillus amyloliquefaciens - isolation & purification</subject><subject>Bacillus amyloliquefaciens - metabolism</subject><subject>Bacteria</subject><subject>Biochemistry</subject><subject>Bioconversion</subject><subject>Biomass</subject><subject>Biotechnology</subject><subject>Carboxymethyl cellulose</subject><subject>Carboxymethylcellulose</subject><subject>Catalysis</subject><subject>Cellulase</subject><subject>Cellulase - biosynthesis</subject><subject>Cellulase - isolation & purification</subject><subject>Cellulase - metabolism</subject><subject>Cellulose</subject><subject>Chelating Agents - pharmacology</subject><subject>Chemical bonds</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Culture Techniques</subject><subject>Disulfide bonds</subject><subject>Edetic acid</subject><subject>Enzyme Stability - drug effects</subject><subject>Enzymes</subject><subject>Ethylenediaminetetraacetic acids</subject><subject>Gel electrophoresis</subject><subject>Glucose</subject><subject>Histidine</subject><subject>Hot springs</subject><subject>Hot Springs - microbiology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolysis</subject><subject>Industry</subject><subject>Ions</subject><subject>Lignocellulose</subject><subject>Lymphocytes B</subject><subject>Metal ions</subject><subject>Metals - pharmacology</subject><subject>Organic chemicals</subject><subject>Organic Chemicals - pharmacology</subject><subject>Organic solvents</subject><subject>Residues</subject><subject>rRNA 16S</subject><subject>Saccharification</subject><subject>Size exclusion chromatography</subject><subject>Sodium dodecyl sulfate</subject><subject>Sodium lauryl sulfate</subject><subject>Solvents</subject><subject>Solvents - pharmacology</subject><subject>Sugar</subject><subject>Surface-Active Agents - pharmacology</subject><subject>Surfactants</subject><subject>Temperature</subject><subject>Temperature effects</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kU9rFTEUxYNY7OvTD-BGAm7cjL33zmRmsqwPbYuFCq3rkGaSOiWT1GSmUJd-ctNOFRFcXTj87rl_DmOvEd4jQHeYkQChAuwqakBU_TO2QSFkBSTxOdsAdXVF1Mt9dpDzDQBSL7oXbJ96rKFruw37-SXFYTHzGAPXYeC7bzppM9s0_tCPYnT8PF3rMBp-Ef2dDXN1Gb1NOsx8Z71fvM6WuxQn_kGbsQiZ6-neRz9-X6wrkg2ZH32W_DRHr2c7rPBJnPnFbRrD9Uu257TP9tVT3bKvnz5e7k6qs_Pj093RWWUakHMlpBEgQbfUoLBEoiGLQyvRXYGTtUFpwZF2iF1twDSu7oTRTpphANk6XW_Zu9X3NsWyWp7VNGZTTtDBxiUr7FvqWiBqC_r2H_QmLimU7RRKamoUVF67ZbhSJsWck3Wq3DPpdK8Q1ENAag1IlYDUQ0CqLz1vnpyXq8kOfzp-J1IAWoH8-Byb_hr9X9dfimCcGg</recordid><startdate>20170801</startdate><enddate>20170801</enddate><creator>Irfan, Muhammad</creator><creator>Tayyab, Ammara</creator><creator>Hasan, Fariha</creator><creator>Khan, Samiullah</creator><creator>Badshah, Malik</creator><creator>Shah, Aamer Ali</creator><general>Springer US</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</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>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope></search><sort><creationdate>20170801</creationdate><title>Production and Characterization of Organic Solvent-Tolerant Cellulase from Bacillus amyloliquefaciens AK9 Isolated from Hot Spring</title><author>Irfan, Muhammad ; Tayyab, Ammara ; Hasan, Fariha ; Khan, Samiullah ; Badshah, Malik ; Shah, Aamer Ali</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-59c5090a62415e22542e1d691fb0f93c19e0f2af1173c0c4f375caf9cdd096fa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Bacillus amyloliquefaciens - 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Academic</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Irfan, Muhammad</au><au>Tayyab, Ammara</au><au>Hasan, Fariha</au><au>Khan, Samiullah</au><au>Badshah, Malik</au><au>Shah, Aamer Ali</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Production and Characterization of Organic Solvent-Tolerant Cellulase from Bacillus amyloliquefaciens AK9 Isolated from Hot Spring</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2017-08-01</date><risdate>2017</risdate><volume>182</volume><issue>4</issue><spage>1390</spage><epage>1402</epage><pages>1390-1402</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><abstract>A cellulase-producing bacterium, designated as strain AK9, was isolated from a hot spring of Tatta Pani, Azad Kashmir, Pakistan. The bacterium was identified as
Bacillus amyloliquefaciens
through 16S rRNA sequencing. Cellulase from strain AK9 was able to liberate glucose from soluble cellulose and carboxymethyl cellulose (CMC). Enzyme was purified through size exclusion chromatography and a single band of ∼47 kDa was observed on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme was purified with recovery of 35.5%, 3.6-fold purity with specific activity of 31 U mg
−1
. The purified cellulase retained its activity over a wide range of temperature (50–70 °C) and pH (3–7) with maximum stability at 60 °C and pH 5.0. The activity inhibited by ethylenediaminetetraacetic acid (EDTA), suggested that it was metalloenzyme. Diethyl pyrocarbonate (DEPC) and β-mercaptoethanol significantly inhibited cellulase activity that revealed the essentiality of histidine residues and disulfide bonds for its catalytic function. It was stable in non-ionic surfactants, in the presence of various metal ions, and in water-insoluble organic solvents. Approximately 9.1% of reducing sugar was released after enzymatic saccharification of DAP-pretreated agro-residue, compared to a very low percentage by autohydrolysis treatment. Hence, it is concluded that cellulase from
B. amyloliquefaciens
AK9 can potentially be used in bioconversion of lignocellulosic biomass to fermentable sugars.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>28130767</pmid><doi>10.1007/s12010-017-2405-8</doi><tpages>13</tpages></addata></record> |
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| ispartof | Applied biochemistry and biotechnology, 2017-08, Vol.182 (4), p.1390-1402 |
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| subjects | Bacillus amyloliquefaciens - growth & development Bacillus amyloliquefaciens - isolation & purification Bacillus amyloliquefaciens - metabolism Bacteria Biochemistry Bioconversion Biomass Biotechnology Carboxymethyl cellulose Carboxymethylcellulose Catalysis Cellulase Cellulase - biosynthesis Cellulase - isolation & purification Cellulase - metabolism Cellulose Chelating Agents - pharmacology Chemical bonds Chemistry Chemistry and Materials Science Culture Techniques Disulfide bonds Edetic acid Enzyme Stability - drug effects Enzymes Ethylenediaminetetraacetic acids Gel electrophoresis Glucose Histidine Hot springs Hot Springs - microbiology Hydrogen-Ion Concentration Hydrolysis Industry Ions Lignocellulose Lymphocytes B Metal ions Metals - pharmacology Organic chemicals Organic Chemicals - pharmacology Organic solvents Residues rRNA 16S Saccharification Size exclusion chromatography Sodium dodecyl sulfate Sodium lauryl sulfate Solvents Solvents - pharmacology Sugar Surface-Active Agents - pharmacology Surfactants Temperature Temperature effects |
| title | Production and Characterization of Organic Solvent-Tolerant Cellulase from Bacillus amyloliquefaciens AK9 Isolated from Hot Spring |
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