Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis
Lytic polysaccharide monooxygenases (LPMOs) are recently discovered oxidative enzymes that are capable of oxidative cleavage of recalcitrant polysaccharides such as chitin or cellulose. Despite the importance of LPMOs in biomass conversion and the large number of lpmo genes in microorganisms, only a...
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| Veröffentlicht in: | International journal of biological macromolecules 2015-08, Vol.79, p.72-75 |
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| creator | Zhang, Huiyan Zhao, Yong Cao, Hailong Mou, Guangqing Yin, Heng |
| description | Lytic polysaccharide monooxygenases (LPMOs) are recently discovered oxidative enzymes that are capable of oxidative cleavage of recalcitrant polysaccharides such as chitin or cellulose. Despite the importance of LPMOs in biomass conversion and the large number of lpmo genes in microorganisms, only a few LPMOs have been well studied, and further characterization of these proteins is thus of interest. In this study, a chitin-active AA10 family LPMO from Bacillus thuringiensis subsp. kurstaki, BtLPMO10A, is described. This enzyme generates even-numbered oxidized oligosaccharides as the dominated products from crystalline chitin, however, interestingly, when colloidal chitin is used as the substrate, a ladder of oxidized oligosaccharides is observed. These results provide new insights into the action mode of LPMOs that may be affected by the substrates. |
| doi_str_mv | 10.1016/j.ijbiomac.2015.04.054 |
| format | Article |
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Despite the importance of LPMOs in biomass conversion and the large number of lpmo genes in microorganisms, only a few LPMOs have been well studied, and further characterization of these proteins is thus of interest. In this study, a chitin-active AA10 family LPMO from Bacillus thuringiensis subsp. kurstaki, BtLPMO10A, is described. This enzyme generates even-numbered oxidized oligosaccharides as the dominated products from crystalline chitin, however, interestingly, when colloidal chitin is used as the substrate, a ladder of oxidized oligosaccharides is observed. 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All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c416t-9eb0e4352244eb6a84ade213c8fd068d276668236aa20778eccc5b72e074a9a83</citedby><cites>FETCH-LOGICAL-c416t-9eb0e4352244eb6a84ade213c8fd068d276668236aa20778eccc5b72e074a9a83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ijbiomac.2015.04.054$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25936286$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Huiyan</creatorcontrib><creatorcontrib>Zhao, Yong</creatorcontrib><creatorcontrib>Cao, Hailong</creatorcontrib><creatorcontrib>Mou, Guangqing</creatorcontrib><creatorcontrib>Yin, Heng</creatorcontrib><title>Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>Lytic polysaccharide monooxygenases (LPMOs) are recently discovered oxidative enzymes that are capable of oxidative cleavage of recalcitrant polysaccharides such as chitin or cellulose. 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These results provide new insights into the action mode of LPMOs that may be affected by the substrates.</description><subject>B. thuringiensis</subject><subject>Bacillus thuringiensis - chemistry</subject><subject>Bacillus thuringiensis - enzymology</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Catalytic Domain</subject><subject>Chitin - chemistry</subject><subject>Cloning, Molecular</subject><subject>Colloids</subject><subject>Crystallization</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Gene Expression</subject><subject>Hydrolysis</subject><subject>Lytic polysaccharide monooxygenases</subject><subject>Mixed Function Oxygenases - chemistry</subject><subject>Mixed Function Oxygenases - genetics</subject><subject>Oligosaccharides - chemistry</subject><subject>Oxidation-Reduction</subject><subject>Polysaccharides</subject><subject>Protein Binding</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Substrate Specificity</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFu2zAMhoViRZO1fYVCx13sSbIsy7dtQbsNKLDLehZomm4V2FYm2UPSp6-DNLvuRODH95Pgx9idFLkU0nze5n7b-DAA5krIMhc6F6W-YGtpqzoTQhQf2FpILTMrC7FiH1PaLqkppb1iK1XWhVHWrBne73eRUvJh5DC2HF8gAk4U_StMxzB0HHh_mDzyXegPCfCI-Jb4EMYQ9odnGiER72IY-DdA3_dz4tPLHP347GlMPt2wyw76RLfv85o9Pdz_3vzIHn99_7n5-pihlmbKamoE6aJUSmtqDFgNLSlZoO1aYWyrKmOMVYUBUKKqLCFi2VSKRKWhBltcs0-nvbsY_syUJjf4hNT3MFKYk5OmrnVdFlW1oOaEYgwpRercLvoB4sFJ4Y6C3dadBbujYCe0WwQvxbv3G3MzUPuvdja6AF9OAC2f_vUUXcJFA1LrI-Hk2uD_d-MNs2CR4w</recordid><startdate>20150801</startdate><enddate>20150801</enddate><creator>Zhang, Huiyan</creator><creator>Zhao, Yong</creator><creator>Cao, Hailong</creator><creator>Mou, Guangqing</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>20150801</creationdate><title>Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis</title><author>Zhang, Huiyan ; Zhao, Yong ; Cao, Hailong ; Mou, Guangqing ; Yin, Heng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c416t-9eb0e4352244eb6a84ade213c8fd068d276668236aa20778eccc5b72e074a9a83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>B. thuringiensis</topic><topic>Bacillus thuringiensis - chemistry</topic><topic>Bacillus thuringiensis - enzymology</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Catalytic Domain</topic><topic>Chitin - chemistry</topic><topic>Cloning, Molecular</topic><topic>Colloids</topic><topic>Crystallization</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Gene Expression</topic><topic>Hydrolysis</topic><topic>Lytic polysaccharide monooxygenases</topic><topic>Mixed Function Oxygenases - chemistry</topic><topic>Mixed Function Oxygenases - genetics</topic><topic>Oligosaccharides - chemistry</topic><topic>Oxidation-Reduction</topic><topic>Polysaccharides</topic><topic>Protein Binding</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Huiyan</creatorcontrib><creatorcontrib>Zhao, Yong</creatorcontrib><creatorcontrib>Cao, Hailong</creatorcontrib><creatorcontrib>Mou, Guangqing</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>Zhang, Huiyan</au><au>Zhao, Yong</au><au>Cao, Hailong</au><au>Mou, Guangqing</au><au>Yin, Heng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis</atitle><jtitle>International journal of biological macromolecules</jtitle><addtitle>Int J Biol Macromol</addtitle><date>2015-08-01</date><risdate>2015</risdate><volume>79</volume><spage>72</spage><epage>75</epage><pages>72-75</pages><issn>0141-8130</issn><eissn>1879-0003</eissn><abstract>Lytic polysaccharide monooxygenases (LPMOs) are recently discovered oxidative enzymes that are capable of oxidative cleavage of recalcitrant polysaccharides such as chitin or cellulose. 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| subjects | B. thuringiensis Bacillus thuringiensis - chemistry Bacillus thuringiensis - enzymology Bacterial Proteins - chemistry Bacterial Proteins - genetics Catalytic Domain Chitin - chemistry Cloning, Molecular Colloids Crystallization Escherichia coli - genetics Escherichia coli - metabolism Gene Expression Hydrolysis Lytic polysaccharide monooxygenases Mixed Function Oxygenases - chemistry Mixed Function Oxygenases - genetics Oligosaccharides - chemistry Oxidation-Reduction Polysaccharides Protein Binding Recombinant Proteins - chemistry Recombinant Proteins - genetics Substrate Specificity |
| title | Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis |
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