Xylanase Isozymes from the Newly Isolated Bacillus sp. CKBx1D and Optimization of Its Deinking Potentiality
Recycling of civic paper waste by enzyme-based technology is nowadays a point of much concern for pollution-less green environment. In this study, the deinking effectiveness of purified xylanase from a newly isolated bacterium was evaluated for recycling of laser jet paper waste. A potent xylanases-...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2012-07, Vol.167 (5), p.1208-1219 |
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| creator | Maity, Chiranjit Ghosh, Kuntal Halder, Suman K. Jana, Arijit Adak, Atanu Das Mohapatra, Pradeep K. Pati, Bikas R. Mondal, Keshab C. |
| description | Recycling of civic paper waste by enzyme-based technology is nowadays a point of much concern for pollution-less green environment. In this study, the deinking effectiveness of purified xylanase from a newly isolated bacterium was evaluated for recycling of laser jet paper waste. A potent xylanases-producing bacterium from the microbial consortia of termite gut was isolated, which was further identified on the basis of 16S rRNA sequence as
Bacillus
sp. CKBx1D. In submerged fermentation condition, the isolate produced the highest level of xylanase (480 U/ml) at 36 h of growth. The extracellular xylanase system comprises of three distinct isozymes (est. Mw 35.28, 28.63, 18.94 kDa). The deinking of laser printed paper waste was performed using the purified enzyme mixture. Whole operational parameters were optimized using the Response Surface Methodology; it was found that at pH 6.8 with 47.2 h of continuous shaking at constant temperature of 35 °C, enzymes showed best deinking activity. After enzyme treatment, the physical properties of the pulp like brightness and ERIC (effective residual ink content) values were enhanced, whereas the pulp opacity was more reduced than the control treatment. Hence, the bacterial isolate and its xylanolytic enzyme system could efficiently be used in recycling paper waste as deinking agent. |
| doi_str_mv | 10.1007/s12010-012-9556-4 |
| format | Article |
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Bacillus
sp. CKBx1D. In submerged fermentation condition, the isolate produced the highest level of xylanase (480 U/ml) at 36 h of growth. The extracellular xylanase system comprises of three distinct isozymes (est. Mw 35.28, 28.63, 18.94 kDa). The deinking of laser printed paper waste was performed using the purified enzyme mixture. Whole operational parameters were optimized using the Response Surface Methodology; it was found that at pH 6.8 with 47.2 h of continuous shaking at constant temperature of 35 °C, enzymes showed best deinking activity. After enzyme treatment, the physical properties of the pulp like brightness and ERIC (effective residual ink content) values were enhanced, whereas the pulp opacity was more reduced than the control treatment. Hence, the bacterial isolate and its xylanolytic enzyme system could efficiently be used in recycling paper waste as deinking agent.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-012-9556-4</identifier><identifier>PMID: 22278053</identifier><language>eng</language><publisher>New York: Springer-Verlag</publisher><subject>Animals ; Bacillus ; Bacillus - classification ; Bacillus - isolation & purification ; Bacillus - metabolism ; Bacteriology ; Biochemistry ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Endo-1,4-beta Xylanases - biosynthesis ; Endo-1,4-beta Xylanases - isolation & purification ; Endo-1,4-beta Xylanases - metabolism ; Enzymes ; Fermentation ; Green Chemistry Technology ; Hydrogen-Ion Concentration ; Ink ; Intestines - microbiology ; Isoenzymes - biosynthesis ; Isoptera ; Isoptera - microbiology ; Models, Theoretical ; Opacity ; Paper industry wastes ; Paper recycling ; Phylogeny ; Physical properties ; Recycling - methods ; Temperature ; Waste disposal</subject><ispartof>Applied biochemistry and biotechnology, 2012-07, Vol.167 (5), p.1208-1219</ispartof><rights>Springer Science+Business Media, LLC 2012</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-901c9fec7505976e0426f476ac9b0182db1de85dd172d9431c4607ec729337ec3</citedby><cites>FETCH-LOGICAL-c405t-901c9fec7505976e0426f476ac9b0182db1de85dd172d9431c4607ec729337ec3</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/s12010-012-9556-4$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-012-9556-4$$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/22278053$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Maity, Chiranjit</creatorcontrib><creatorcontrib>Ghosh, Kuntal</creatorcontrib><creatorcontrib>Halder, Suman K.</creatorcontrib><creatorcontrib>Jana, Arijit</creatorcontrib><creatorcontrib>Adak, Atanu</creatorcontrib><creatorcontrib>Das Mohapatra, Pradeep K.</creatorcontrib><creatorcontrib>Pati, Bikas R.</creatorcontrib><creatorcontrib>Mondal, Keshab C.</creatorcontrib><title>Xylanase Isozymes from the Newly Isolated Bacillus sp. CKBx1D and Optimization of Its Deinking Potentiality</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>Recycling of civic paper waste by enzyme-based technology is nowadays a point of much concern for pollution-less green environment. In this study, the deinking effectiveness of purified xylanase from a newly isolated bacterium was evaluated for recycling of laser jet paper waste. A potent xylanases-producing bacterium from the microbial consortia of termite gut was isolated, which was further identified on the basis of 16S rRNA sequence as
Bacillus
sp. CKBx1D. In submerged fermentation condition, the isolate produced the highest level of xylanase (480 U/ml) at 36 h of growth. The extracellular xylanase system comprises of three distinct isozymes (est. Mw 35.28, 28.63, 18.94 kDa). The deinking of laser printed paper waste was performed using the purified enzyme mixture. Whole operational parameters were optimized using the Response Surface Methodology; it was found that at pH 6.8 with 47.2 h of continuous shaking at constant temperature of 35 °C, enzymes showed best deinking activity. After enzyme treatment, the physical properties of the pulp like brightness and ERIC (effective residual ink content) values were enhanced, whereas the pulp opacity was more reduced than the control treatment. Hence, the bacterial isolate and its xylanolytic enzyme system could efficiently be used in recycling paper waste as deinking agent.</description><subject>Animals</subject><subject>Bacillus</subject><subject>Bacillus - classification</subject><subject>Bacillus - isolation & purification</subject><subject>Bacillus - metabolism</subject><subject>Bacteriology</subject><subject>Biochemistry</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Endo-1,4-beta Xylanases - biosynthesis</subject><subject>Endo-1,4-beta Xylanases - isolation & purification</subject><subject>Endo-1,4-beta Xylanases - metabolism</subject><subject>Enzymes</subject><subject>Fermentation</subject><subject>Green Chemistry Technology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Ink</subject><subject>Intestines - microbiology</subject><subject>Isoenzymes - biosynthesis</subject><subject>Isoptera</subject><subject>Isoptera - microbiology</subject><subject>Models, Theoretical</subject><subject>Opacity</subject><subject>Paper industry wastes</subject><subject>Paper recycling</subject><subject>Phylogeny</subject><subject>Physical properties</subject><subject>Recycling - methods</subject><subject>Temperature</subject><subject>Waste disposal</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</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>eNqNkcFu1DAQhi1URLeFB-BSWeqFS8qME8fxsd1tYcWKcgCJW-RNJq3bJN7Gjmj69HjZBaFKSJxGsr_57ZmPsbcIZwig3nsUgJAAikRLmSfZCzZDKXUCQuMBm4FQaSJEoQ_Zkfd3EMFCqlfsUAihCpDpjN1_n1rTG0986d3T1JHnzeA6Hm6Jf6Yf7bQ9b02gml-Yyrbt6LnfnPH5p4tHXHDT1_x6E2xnn0ywrueu4cvg-YJsf2_7G_7FBeqDNa0N02v2sjGtpzf7esy-XV1-nX9MVtcflvPzVVJlIEOiASvdUKUkSK1ygkzkTaZyU-k1YCHqNdZUyLpGJWqdpVhlOajIC52msabH7N0udzO4h5F8KDvrK2rjoORGXyKkcSeIoP4DjStUEL8U0dNn6J0bhz4O8ouKBBRbCndUNTjvB2rKzWA7M0wRKrfSyp20Mroot9LKLPac7JPHdUf1n47fliIgdoCPV_0NDX8__a_Un9OSn7M</recordid><startdate>20120701</startdate><enddate>20120701</enddate><creator>Maity, Chiranjit</creator><creator>Ghosh, Kuntal</creator><creator>Halder, Suman K.</creator><creator>Jana, Arijit</creator><creator>Adak, Atanu</creator><creator>Das Mohapatra, Pradeep K.</creator><creator>Pati, Bikas R.</creator><creator>Mondal, Keshab C.</creator><general>Springer-Verlag</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><scope>7QL</scope><scope>7QO</scope></search><sort><creationdate>20120701</creationdate><title>Xylanase Isozymes from the Newly Isolated Bacillus sp. 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microbiology</topic><topic>Isoenzymes - biosynthesis</topic><topic>Isoptera</topic><topic>Isoptera - microbiology</topic><topic>Models, Theoretical</topic><topic>Opacity</topic><topic>Paper industry wastes</topic><topic>Paper recycling</topic><topic>Phylogeny</topic><topic>Physical properties</topic><topic>Recycling - methods</topic><topic>Temperature</topic><topic>Waste disposal</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Maity, Chiranjit</creatorcontrib><creatorcontrib>Ghosh, Kuntal</creatorcontrib><creatorcontrib>Halder, Suman K.</creatorcontrib><creatorcontrib>Jana, Arijit</creatorcontrib><creatorcontrib>Adak, Atanu</creatorcontrib><creatorcontrib>Das Mohapatra, Pradeep K.</creatorcontrib><creatorcontrib>Pati, Bikas R.</creatorcontrib><creatorcontrib>Mondal, Keshab C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - 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Bacillus
sp. CKBx1D. In submerged fermentation condition, the isolate produced the highest level of xylanase (480 U/ml) at 36 h of growth. The extracellular xylanase system comprises of three distinct isozymes (est. Mw 35.28, 28.63, 18.94 kDa). The deinking of laser printed paper waste was performed using the purified enzyme mixture. Whole operational parameters were optimized using the Response Surface Methodology; it was found that at pH 6.8 with 47.2 h of continuous shaking at constant temperature of 35 °C, enzymes showed best deinking activity. After enzyme treatment, the physical properties of the pulp like brightness and ERIC (effective residual ink content) values were enhanced, whereas the pulp opacity was more reduced than the control treatment. Hence, the bacterial isolate and its xylanolytic enzyme system could efficiently be used in recycling paper waste as deinking agent.</abstract><cop>New York</cop><pub>Springer-Verlag</pub><pmid>22278053</pmid><doi>10.1007/s12010-012-9556-4</doi><tpages>12</tpages></addata></record> |
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| subjects | Animals Bacillus Bacillus - classification Bacillus - isolation & purification Bacillus - metabolism Bacteriology Biochemistry Biotechnology Chemistry Chemistry and Materials Science Endo-1,4-beta Xylanases - biosynthesis Endo-1,4-beta Xylanases - isolation & purification Endo-1,4-beta Xylanases - metabolism Enzymes Fermentation Green Chemistry Technology Hydrogen-Ion Concentration Ink Intestines - microbiology Isoenzymes - biosynthesis Isoptera Isoptera - microbiology Models, Theoretical Opacity Paper industry wastes Paper recycling Phylogeny Physical properties Recycling - methods Temperature Waste disposal |
| title | Xylanase Isozymes from the Newly Isolated Bacillus sp. CKBx1D and Optimization of Its Deinking Potentiality |
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