Optimization of Conditions for Maximal Production of Recombinant Thermostable Cellulase from Thermotoga naphthophila using E. coli BL21-CodonPlus (DE3) as Expression Host
ABSTRACT Current study was designed for the development of an economic and environment friendly mechanism for the production of thermostable cellulase. Production of cellulase was focused due to its diverse range of application in industry. In the present study, conditions were optimized for the max...
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| Veröffentlicht in: | Pakistan journal of zoology 2019-08, Vol.51 (4), p.1371 |
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| container_title | Pakistan journal of zoology |
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| creator | Khalid, Aisha Tayyab, Muhammad Hashmi, Abu Saeed Yaqub, Tahir Awan, Ali Raza Wasim, Muhammad Saeed, Shagufta Firyal, Sehrish Shakoori, Abdul Rauf |
| description | ABSTRACT Current study was designed for the development of an economic and environment friendly mechanism for the production of thermostable cellulase. Production of cellulase was focused due to its diverse range of application in industry. In the present study, conditions were optimized for the maximal production of recombinant thermostable cellulase from Thermotoga naphthophila using BL21-CodonPlus (DE3) cells as expression host and pET28a as expression vector. Effect of various concentration of Isopropyl β-D-1-thiogalactopyranoside (IPTG), post induction time, effect of temperature and pH were examined for the maximal production of recombinant cellulase. The effect of supplementation of LB medium with additional carbon and nitrogen sources was also analyzed for maximal production of recombinant protein. Higher level enzyme activity was recorded at 25°C, pH 7.0 when the cells were induced with 0.5 mM IPTG with 22h post induction incubation. Supplementation of LB medium with 1% glucose and yeast extract enhanced the production of recombinant thermostable cellulase. Enzyme showed strong potential for its use in paper and poultry feed industry. Under the optimal conditions we could able to produce 48 U/mL of recombinant cellulase. |
| doi_str_mv | 10.17582/journal.pjz/2019.51.4.1371.1377 |
| format | Article |
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Production of cellulase was focused due to its diverse range of application in industry. In the present study, conditions were optimized for the maximal production of recombinant thermostable cellulase from Thermotoga naphthophila using BL21-CodonPlus (DE3) cells as expression host and pET28a as expression vector. Effect of various concentration of Isopropyl β-D-1-thiogalactopyranoside (IPTG), post induction time, effect of temperature and pH were examined for the maximal production of recombinant cellulase. The effect of supplementation of LB medium with additional carbon and nitrogen sources was also analyzed for maximal production of recombinant protein. Higher level enzyme activity was recorded at 25°C, pH 7.0 when the cells were induced with 0.5 mM IPTG with 22h post induction incubation. Supplementation of LB medium with 1% glucose and yeast extract enhanced the production of recombinant thermostable cellulase. Enzyme showed strong potential for its use in paper and poultry feed industry. Under the optimal conditions we could able to produce 48 U/mL of recombinant cellulase.</description><identifier>ISSN: 0030-9923</identifier><identifier>DOI: 10.17582/journal.pjz/2019.51.4.1371.1377</identifier><language>eng</language><publisher>Lahore: Knowledge Bylanes</publisher><subject>Anopheles ; Carbon ; Carbon sources ; Cellulase ; Cellulose ; E coli ; Enzymatic activity ; Enzyme activity ; Enzymes ; Escherichia coli ; Feed industry ; Glucose ; Hydrolysis ; Industrial applications ; Lactose ; Microbiological research ; Nitrogen ; Nitrogen sources ; Optimization ; pH effects ; Polymer industry ; Polymers ; Polysaccharides ; Poultry feed ; Proteins ; Recombinant proteins ; Temperature effects ; Thermotoga naphthophila ; Thermotogales ; Yeasts</subject><ispartof>Pakistan journal of zoology, 2019-08, Vol.51 (4), p.1371</ispartof><rights>COPYRIGHT 2019 Knowledge Bylanes</rights><rights>(c)2019 Pakistan Journal of Zoology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c330t-12b7052dd88f71cf3ffb88dba3555784f0a6b2fd8d408995bd29f914493a15c43</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Khalid, Aisha</creatorcontrib><creatorcontrib>Tayyab, Muhammad</creatorcontrib><creatorcontrib>Hashmi, Abu Saeed</creatorcontrib><creatorcontrib>Yaqub, Tahir</creatorcontrib><creatorcontrib>Awan, Ali Raza</creatorcontrib><creatorcontrib>Wasim, Muhammad</creatorcontrib><creatorcontrib>Saeed, Shagufta</creatorcontrib><creatorcontrib>Firyal, Sehrish</creatorcontrib><creatorcontrib>Shakoori, Abdul Rauf</creatorcontrib><title>Optimization of Conditions for Maximal Production of Recombinant Thermostable Cellulase from Thermotoga naphthophila using E. coli BL21-CodonPlus (DE3) as Expression Host</title><title>Pakistan journal of zoology</title><description>ABSTRACT Current study was designed for the development of an economic and environment friendly mechanism for the production of thermostable cellulase. Production of cellulase was focused due to its diverse range of application in industry. In the present study, conditions were optimized for the maximal production of recombinant thermostable cellulase from Thermotoga naphthophila using BL21-CodonPlus (DE3) cells as expression host and pET28a as expression vector. Effect of various concentration of Isopropyl β-D-1-thiogalactopyranoside (IPTG), post induction time, effect of temperature and pH were examined for the maximal production of recombinant cellulase. The effect of supplementation of LB medium with additional carbon and nitrogen sources was also analyzed for maximal production of recombinant protein. Higher level enzyme activity was recorded at 25°C, pH 7.0 when the cells were induced with 0.5 mM IPTG with 22h post induction incubation. Supplementation of LB medium with 1% glucose and yeast extract enhanced the production of recombinant thermostable cellulase. Enzyme showed strong potential for its use in paper and poultry feed industry. Under the optimal conditions we could able to produce 48 U/mL of recombinant cellulase.</description><subject>Anopheles</subject><subject>Carbon</subject><subject>Carbon sources</subject><subject>Cellulase</subject><subject>Cellulose</subject><subject>E coli</subject><subject>Enzymatic activity</subject><subject>Enzyme activity</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Feed industry</subject><subject>Glucose</subject><subject>Hydrolysis</subject><subject>Industrial applications</subject><subject>Lactose</subject><subject>Microbiological research</subject><subject>Nitrogen</subject><subject>Nitrogen sources</subject><subject>Optimization</subject><subject>pH effects</subject><subject>Polymer industry</subject><subject>Polymers</subject><subject>Polysaccharides</subject><subject>Poultry feed</subject><subject>Proteins</subject><subject>Recombinant proteins</subject><subject>Temperature effects</subject><subject>Thermotoga naphthophila</subject><subject>Thermotogales</subject><subject>Yeasts</subject><issn>0030-9923</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNo1UU1r3DAQ9aGFhjT_QdBLerCjD2st3Zq626awJaGkZyFb0q4WWXIlGdL8pP7KyNnNDMwwM2_mwbyqukawQR1l-OYYluila-bj8w2GiDcUNW2DSIfW0L2rLiAksOYckw_VVUpHWKzdUIzZRfX_fs52ss8y2-BBMKAPXtm1SMCECH7JJztJBx5iUMv4BvqtxzAN1kufweNBxymkLAenQa-dW5xMGpgYpvMsh70EXs6HfAjzwToJlmT9HmwbMAZnwdcdRnUfVPAPbkng-tuWfAYyge3THHVKK-ddIfhYvTfSJX11zpfVn-_bx_6u3t3_-Nnf7uqREJhrhIcOUqwUY6ZDoyHGDIypQRJKacdaA-VmwEYx1ULGOR0U5oajtuVEIjq25LL6dLo7x_B30SmL84eTwIQSyjGDtKCaE2ovnRbWm5CjHIsrPdkxeG1s6d9SzjfFOCoLX04LYwwpRW3EHMtr4z-BoHhV8o1HFCXFqqSgSLRiVXINHXkBPSuaPQ</recordid><startdate>20190831</startdate><enddate>20190831</enddate><creator>Khalid, Aisha</creator><creator>Tayyab, Muhammad</creator><creator>Hashmi, Abu Saeed</creator><creator>Yaqub, Tahir</creator><creator>Awan, Ali Raza</creator><creator>Wasim, Muhammad</creator><creator>Saeed, Shagufta</creator><creator>Firyal, Sehrish</creator><creator>Shakoori, Abdul Rauf</creator><general>Knowledge Bylanes</general><general>AsiaNet Pakistan (Pvt) Ltd</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7SS</scope><scope>7XB</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PATMY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>RC3</scope></search><sort><creationdate>20190831</creationdate><title>Optimization of Conditions for Maximal Production of Recombinant Thermostable Cellulase from Thermotoga naphthophila using E. coli BL21-CodonPlus (DE3) as Expression Host</title><author>Khalid, Aisha ; Tayyab, Muhammad ; Hashmi, Abu Saeed ; Yaqub, Tahir ; Awan, Ali Raza ; Wasim, Muhammad ; Saeed, Shagufta ; Firyal, Sehrish ; Shakoori, Abdul Rauf</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c330t-12b7052dd88f71cf3ffb88dba3555784f0a6b2fd8d408995bd29f914493a15c43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Anopheles</topic><topic>Carbon</topic><topic>Carbon sources</topic><topic>Cellulase</topic><topic>Cellulose</topic><topic>E coli</topic><topic>Enzymatic activity</topic><topic>Enzyme activity</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Feed industry</topic><topic>Glucose</topic><topic>Hydrolysis</topic><topic>Industrial applications</topic><topic>Lactose</topic><topic>Microbiological research</topic><topic>Nitrogen</topic><topic>Nitrogen sources</topic><topic>Optimization</topic><topic>pH effects</topic><topic>Polymer industry</topic><topic>Polymers</topic><topic>Polysaccharides</topic><topic>Poultry feed</topic><topic>Proteins</topic><topic>Recombinant proteins</topic><topic>Temperature effects</topic><topic>Thermotoga naphthophila</topic><topic>Thermotogales</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Khalid, Aisha</creatorcontrib><creatorcontrib>Tayyab, Muhammad</creatorcontrib><creatorcontrib>Hashmi, Abu Saeed</creatorcontrib><creatorcontrib>Yaqub, Tahir</creatorcontrib><creatorcontrib>Awan, Ali Raza</creatorcontrib><creatorcontrib>Wasim, Muhammad</creatorcontrib><creatorcontrib>Saeed, Shagufta</creatorcontrib><creatorcontrib>Firyal, Sehrish</creatorcontrib><creatorcontrib>Shakoori, Abdul Rauf</creatorcontrib><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><jtitle>Pakistan journal of zoology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Khalid, Aisha</au><au>Tayyab, Muhammad</au><au>Hashmi, Abu Saeed</au><au>Yaqub, Tahir</au><au>Awan, Ali Raza</au><au>Wasim, Muhammad</au><au>Saeed, Shagufta</au><au>Firyal, Sehrish</au><au>Shakoori, Abdul Rauf</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Optimization of Conditions for Maximal Production of Recombinant Thermostable Cellulase from Thermotoga naphthophila using E. coli BL21-CodonPlus (DE3) as Expression Host</atitle><jtitle>Pakistan journal of zoology</jtitle><date>2019-08-31</date><risdate>2019</risdate><volume>51</volume><issue>4</issue><spage>1371</spage><pages>1371-</pages><issn>0030-9923</issn><abstract>ABSTRACT Current study was designed for the development of an economic and environment friendly mechanism for the production of thermostable cellulase. Production of cellulase was focused due to its diverse range of application in industry. In the present study, conditions were optimized for the maximal production of recombinant thermostable cellulase from Thermotoga naphthophila using BL21-CodonPlus (DE3) cells as expression host and pET28a as expression vector. Effect of various concentration of Isopropyl β-D-1-thiogalactopyranoside (IPTG), post induction time, effect of temperature and pH were examined for the maximal production of recombinant cellulase. The effect of supplementation of LB medium with additional carbon and nitrogen sources was also analyzed for maximal production of recombinant protein. Higher level enzyme activity was recorded at 25°C, pH 7.0 when the cells were induced with 0.5 mM IPTG with 22h post induction incubation. Supplementation of LB medium with 1% glucose and yeast extract enhanced the production of recombinant thermostable cellulase. Enzyme showed strong potential for its use in paper and poultry feed industry. Under the optimal conditions we could able to produce 48 U/mL of recombinant cellulase.</abstract><cop>Lahore</cop><pub>Knowledge Bylanes</pub><doi>10.17582/journal.pjz/2019.51.4.1371.1377</doi><oa>free_for_read</oa></addata></record> |
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| ispartof | Pakistan journal of zoology, 2019-08, Vol.51 (4), p.1371 |
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| language | eng |
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| source | EZB-FREE-00999 freely available EZB journals |
| subjects | Anopheles Carbon Carbon sources Cellulase Cellulose E coli Enzymatic activity Enzyme activity Enzymes Escherichia coli Feed industry Glucose Hydrolysis Industrial applications Lactose Microbiological research Nitrogen Nitrogen sources Optimization pH effects Polymer industry Polymers Polysaccharides Poultry feed Proteins Recombinant proteins Temperature effects Thermotoga naphthophila Thermotogales Yeasts |
| title | Optimization of Conditions for Maximal Production of Recombinant Thermostable Cellulase from Thermotoga naphthophila using E. coli BL21-CodonPlus (DE3) as Expression Host |
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