Characterisation of a chitinase from Pseudoalteromonas sp. DL-6, a marine psychrophilic bacterium
In this study, we isolated a new psychrophilic bacterium, Pseudoalteromonas sp. DL-6 from marine sediments, which grew well on chitin-containing plates at 4°C. One endo-type chitinase gene, chiA, was cloned from the genomic DNA of this bacterium and heterologously expressed in Escherichia coli BL21...
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| Veröffentlicht in: | International journal of biological macromolecules 2014-09, Vol.70, p.455-462 |
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| creator | Wang, Xiaohui Zhao, Yong Tan, Haidong Chi, Naiyu Zhang, Qingfang Du, Yuguang Yin, Heng |
| description | In this study, we isolated a new psychrophilic bacterium, Pseudoalteromonas sp. DL-6 from marine sediments, which grew well on chitin-containing plates at 4°C. One endo-type chitinase gene, chiA, was cloned from the genomic DNA of this bacterium and heterologously expressed in Escherichia coli BL21 (DE3). ChiA showed very high catalytic activity, even at 4°C, and exhibited maximal activity on a chitinous substrate at pH 8.0 and 20°C. Kinetic studies indicated that ChiA has a greater catalytic efficiency on 4-methylumbelliferyl-β-d-N,N′,N″-triacetylchitotriose[4-MU(GlcNAc)3] than on 4-methylumbelliferyl-β-d-N,N′-diacetylchitobioside[4-MU(GlcNAc)2]. Electrospray ionisation mass spectrometry (ESI-MS) analysis showed that the hydrolysis products of powdered chitin after ChiA digestion consisted of a series of chitin oligomers with different degrees of polymerisation. The ChiA mode of action was also examined using (GlcNAc)2–6 as a substrate, and the results suggested that ChiA is a non-processive endo-type chitinase. |
| doi_str_mv | 10.1016/j.ijbiomac.2014.07.033 |
| format | Article |
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DL-6, a marine psychrophilic bacterium</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Wang, Xiaohui ; Zhao, Yong ; Tan, Haidong ; Chi, Naiyu ; Zhang, Qingfang ; Du, Yuguang ; Yin, Heng</creator><creatorcontrib>Wang, Xiaohui ; Zhao, Yong ; Tan, Haidong ; Chi, Naiyu ; Zhang, Qingfang ; Du, Yuguang ; Yin, Heng</creatorcontrib><description>In this study, we isolated a new psychrophilic bacterium, Pseudoalteromonas sp. DL-6 from marine sediments, which grew well on chitin-containing plates at 4°C. One endo-type chitinase gene, chiA, was cloned from the genomic DNA of this bacterium and heterologously expressed in Escherichia coli BL21 (DE3). ChiA showed very high catalytic activity, even at 4°C, and exhibited maximal activity on a chitinous substrate at pH 8.0 and 20°C. Kinetic studies indicated that ChiA has a greater catalytic efficiency on 4-methylumbelliferyl-β-d-N,N′,N″-triacetylchitotriose[4-MU(GlcNAc)3] than on 4-methylumbelliferyl-β-d-N,N′-diacetylchitobioside[4-MU(GlcNAc)2]. Electrospray ionisation mass spectrometry (ESI-MS) analysis showed that the hydrolysis products of powdered chitin after ChiA digestion consisted of a series of chitin oligomers with different degrees of polymerisation. The ChiA mode of action was also examined using (GlcNAc)2–6 as a substrate, and the results suggested that ChiA is a non-processive endo-type chitinase.</description><identifier>ISSN: 0141-8130</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2014.07.033</identifier><identifier>PMID: 25064555</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Characterisation ; Chitin - metabolism ; Chitinase ; Chitinases - chemistry ; Chitinases - genetics ; Chitinases - metabolism ; Cloning, Molecular ; Enzyme Activation ; Gene Expression ; Hydrogen-Ion Concentration ; Hydrolysis ; Kinetics ; Pseudoalteromonas - classification ; Pseudoalteromonas - enzymology ; Pseudoalteromonas - genetics ; Purification ; Substrate Specificity ; Temperature</subject><ispartof>International journal of biological macromolecules, 2014-09, Vol.70, p.455-462</ispartof><rights>2014 Elsevier B.V.</rights><rights>Copyright © 2014 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-cfffc5baedea719b7d2edeec43ce5efae67ff0ba1f6af0c00b7f769bfcfcff453</citedby><cites>FETCH-LOGICAL-c368t-cfffc5baedea719b7d2edeec43ce5efae67ff0ba1f6af0c00b7f769bfcfcff453</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S014181301400508X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25064555$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Xiaohui</creatorcontrib><creatorcontrib>Zhao, Yong</creatorcontrib><creatorcontrib>Tan, Haidong</creatorcontrib><creatorcontrib>Chi, Naiyu</creatorcontrib><creatorcontrib>Zhang, Qingfang</creatorcontrib><creatorcontrib>Du, Yuguang</creatorcontrib><creatorcontrib>Yin, Heng</creatorcontrib><title>Characterisation of a chitinase from Pseudoalteromonas sp. DL-6, a marine psychrophilic bacterium</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>In this study, we isolated a new psychrophilic bacterium, Pseudoalteromonas sp. DL-6 from marine sediments, which grew well on chitin-containing plates at 4°C. One endo-type chitinase gene, chiA, was cloned from the genomic DNA of this bacterium and heterologously expressed in Escherichia coli BL21 (DE3). ChiA showed very high catalytic activity, even at 4°C, and exhibited maximal activity on a chitinous substrate at pH 8.0 and 20°C. Kinetic studies indicated that ChiA has a greater catalytic efficiency on 4-methylumbelliferyl-β-d-N,N′,N″-triacetylchitotriose[4-MU(GlcNAc)3] than on 4-methylumbelliferyl-β-d-N,N′-diacetylchitobioside[4-MU(GlcNAc)2]. Electrospray ionisation mass spectrometry (ESI-MS) analysis showed that the hydrolysis products of powdered chitin after ChiA digestion consisted of a series of chitin oligomers with different degrees of polymerisation. The ChiA mode of action was also examined using (GlcNAc)2–6 as a substrate, and the results suggested that ChiA is a non-processive endo-type chitinase.</description><subject>Characterisation</subject><subject>Chitin - metabolism</subject><subject>Chitinase</subject><subject>Chitinases - chemistry</subject><subject>Chitinases - genetics</subject><subject>Chitinases - metabolism</subject><subject>Cloning, Molecular</subject><subject>Enzyme Activation</subject><subject>Gene Expression</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolysis</subject><subject>Kinetics</subject><subject>Pseudoalteromonas - classification</subject><subject>Pseudoalteromonas - enzymology</subject><subject>Pseudoalteromonas - genetics</subject><subject>Purification</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtPwzAMgCMEgvH4CyhHDrQk65KsN9B4SpPgAOcodR0tU9uUpEXavydTgSvyIZbz2ZY_Qi45yznj8mabu23lfGsgnzO-yJnKWVEckBlfqjJjjBWHZJY-eLbkBTshpzFuU1UKvjwmJ3PB5EIIMSNmtTHBwIDBRTM431FvqaGwcYPrTERqg2_pW8Sx9qZJmG99qtPY5_R-ncnrBLcmuA5pH3ewCb7fuMYBraahY3tOjqxpIl78vGfk4_HhffWcrV-fXlZ36wwKuRwysNaCqAzWaBQvK1XPU4qwKAAFWoNSWcsqw600lgFjlbJKlpWFFHYhijNyNc3tg_8cMQ66dRGwaUyHfoyaC1FKrpQoEyonFIKPMaDVfXDpip3mTO_16q3-1av3ejVTOulNjZc_O8aqxfqv7ddnAm4nANOlXw6DjuCwA6xdQBh07d1_O74BE6eSpw</recordid><startdate>20140901</startdate><enddate>20140901</enddate><creator>Wang, Xiaohui</creator><creator>Zhao, Yong</creator><creator>Tan, Haidong</creator><creator>Chi, Naiyu</creator><creator>Zhang, Qingfang</creator><creator>Du, Yuguang</creator><creator>Yin, Heng</creator><general>Elsevier 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>7X8</scope></search><sort><creationdate>20140901</creationdate><title>Characterisation of a chitinase from Pseudoalteromonas sp. DL-6, a marine psychrophilic bacterium</title><author>Wang, Xiaohui ; Zhao, Yong ; Tan, Haidong ; Chi, Naiyu ; Zhang, Qingfang ; Du, Yuguang ; Yin, Heng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-cfffc5baedea719b7d2edeec43ce5efae67ff0ba1f6af0c00b7f769bfcfcff453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Characterisation</topic><topic>Chitin - metabolism</topic><topic>Chitinase</topic><topic>Chitinases - chemistry</topic><topic>Chitinases - genetics</topic><topic>Chitinases - metabolism</topic><topic>Cloning, Molecular</topic><topic>Enzyme Activation</topic><topic>Gene Expression</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolysis</topic><topic>Kinetics</topic><topic>Pseudoalteromonas - classification</topic><topic>Pseudoalteromonas - enzymology</topic><topic>Pseudoalteromonas - genetics</topic><topic>Purification</topic><topic>Substrate Specificity</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Xiaohui</creatorcontrib><creatorcontrib>Zhao, Yong</creatorcontrib><creatorcontrib>Tan, Haidong</creatorcontrib><creatorcontrib>Chi, Naiyu</creatorcontrib><creatorcontrib>Zhang, Qingfang</creatorcontrib><creatorcontrib>Du, Yuguang</creatorcontrib><creatorcontrib>Yin, Heng</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Xiaohui</au><au>Zhao, Yong</au><au>Tan, Haidong</au><au>Chi, Naiyu</au><au>Zhang, Qingfang</au><au>Du, Yuguang</au><au>Yin, Heng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterisation of a chitinase from Pseudoalteromonas sp. 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Electrospray ionisation mass spectrometry (ESI-MS) analysis showed that the hydrolysis products of powdered chitin after ChiA digestion consisted of a series of chitin oligomers with different degrees of polymerisation. The ChiA mode of action was also examined using (GlcNAc)2–6 as a substrate, and the results suggested that ChiA is a non-processive endo-type chitinase.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>25064555</pmid><doi>10.1016/j.ijbiomac.2014.07.033</doi><tpages>8</tpages></addata></record> |
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| subjects | Characterisation Chitin - metabolism Chitinase Chitinases - chemistry Chitinases - genetics Chitinases - metabolism Cloning, Molecular Enzyme Activation Gene Expression Hydrogen-Ion Concentration Hydrolysis Kinetics Pseudoalteromonas - classification Pseudoalteromonas - enzymology Pseudoalteromonas - genetics Purification Substrate Specificity Temperature |
| title | Characterisation of a chitinase from Pseudoalteromonas sp. DL-6, a marine psychrophilic bacterium |
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