Chitooligosaccharides are converted to N-acetylglucosamine by N-acetyl-β-hexosaminidase from Stenotrophomonas maltophilia
Abstract The Stenotrophomonas maltophilia k279a (Stm) Hex gene encodes a polypeptide of 785 amino acid residues, with an N-terminal signal peptide. StmHex was cloned without signal peptide and expressed as an 83.6 kDa soluble protein in Escherichia coli BL21 (DE3). Purified StmHex was optimally acti...
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| Veröffentlicht in: | FEMS microbiology letters 2013-11, Vol.348 (1), p.19-25 |
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| creator | Katta, Suma Ankati, Sravani Podile, Appa Rao |
| description | Abstract
The Stenotrophomonas maltophilia k279a (Stm) Hex gene encodes a polypeptide of 785 amino acid residues, with an N-terminal signal peptide. StmHex was cloned without signal peptide and expressed as an 83.6 kDa soluble protein in Escherichia coli BL21 (DE3). Purified StmHex was optimally active at pH 5.0 and 40 °C. The Vmax, Km and kcat/Km for StmHex towards chitin hexamer were 10.55 nkat (mg protein)−1, 271 μM and 0.246 s−1 mM−1, while the kinetic values with chitobiose were 30.65 nkat (mg protein)−1, 2365 μM and 0.082 s−1 mM−1, respectively. Hydrolytic activity on chitooligosaccharides indicated that StmHex was an exo-acting enzyme and yielded N-acetyl-d-glucosamine (GlcNAc) as the final product. StmHex hydrolysed chitooligosaccharides (up to hexamer) into GlcNAc within 60 min, suggesting that this enzyme has potential for use in large-scale production of GlcNAc from chitooligosaccharides. |
| doi_str_mv | 10.1111/1574-6968.12237 |
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The Stenotrophomonas maltophilia k279a (Stm) Hex gene encodes a polypeptide of 785 amino acid residues, with an N-terminal signal peptide. StmHex was cloned without signal peptide and expressed as an 83.6 kDa soluble protein in Escherichia coli BL21 (DE3). Purified StmHex was optimally active at pH 5.0 and 40 °C. The Vmax, Km and kcat/Km for StmHex towards chitin hexamer were 10.55 nkat (mg protein)−1, 271 μM and 0.246 s−1 mM−1, while the kinetic values with chitobiose were 30.65 nkat (mg protein)−1, 2365 μM and 0.082 s−1 mM−1, respectively. Hydrolytic activity on chitooligosaccharides indicated that StmHex was an exo-acting enzyme and yielded N-acetyl-d-glucosamine (GlcNAc) as the final product. StmHex hydrolysed chitooligosaccharides (up to hexamer) into GlcNAc within 60 min, suggesting that this enzyme has potential for use in large-scale production of GlcNAc from chitooligosaccharides.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/1574-6968.12237</identifier><identifier>PMID: 23965017</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Acetylglucosamine - metabolism ; Bacteriology ; beta-N-Acetylhexosaminidases - chemistry ; beta-N-Acetylhexosaminidases - genetics ; beta-N-Acetylhexosaminidases - isolation & purification ; beta-N-Acetylhexosaminidases - metabolism ; Biological and medical sciences ; chitooligosaccharides ; Chitosan - metabolism ; Cloning, Molecular ; Enzyme Stability ; Escherichia coli ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Kinetics ; Microbiology ; Miscellaneous ; Molecular Weight ; N‐acetylhexosaminidase ; Oligosaccharides - metabolism ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Stenotrophomonas maltophilia ; Stenotrophomonas maltophilia - enzymology ; Stenotrophomonas maltophilia - genetics ; Temperature</subject><ispartof>FEMS microbiology letters, 2013-11, Vol.348 (1), p.19-25</ispartof><rights>2013 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved 2013</rights><rights>2013 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved</rights><rights>2014 INIST-CNRS</rights><rights>2013 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4417-a0377f6e4518d902d70ebafa84ddcbc7d868cbc6f8c271e6b86430c5f74fb0f53</citedby><cites>FETCH-LOGICAL-c4417-a0377f6e4518d902d70ebafa84ddcbc7d868cbc6f8c271e6b86430c5f74fb0f53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2F1574-6968.12237$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2F1574-6968.12237$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=27822746$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23965017$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Katta, Suma</creatorcontrib><creatorcontrib>Ankati, Sravani</creatorcontrib><creatorcontrib>Podile, Appa Rao</creatorcontrib><title>Chitooligosaccharides are converted to N-acetylglucosamine by N-acetyl-β-hexosaminidase from Stenotrophomonas maltophilia</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
The Stenotrophomonas maltophilia k279a (Stm) Hex gene encodes a polypeptide of 785 amino acid residues, with an N-terminal signal peptide. StmHex was cloned without signal peptide and expressed as an 83.6 kDa soluble protein in Escherichia coli BL21 (DE3). Purified StmHex was optimally active at pH 5.0 and 40 °C. The Vmax, Km and kcat/Km for StmHex towards chitin hexamer were 10.55 nkat (mg protein)−1, 271 μM and 0.246 s−1 mM−1, while the kinetic values with chitobiose were 30.65 nkat (mg protein)−1, 2365 μM and 0.082 s−1 mM−1, respectively. Hydrolytic activity on chitooligosaccharides indicated that StmHex was an exo-acting enzyme and yielded N-acetyl-d-glucosamine (GlcNAc) as the final product. StmHex hydrolysed chitooligosaccharides (up to hexamer) into GlcNAc within 60 min, suggesting that this enzyme has potential for use in large-scale production of GlcNAc from chitooligosaccharides.</description><subject>Acetylglucosamine - metabolism</subject><subject>Bacteriology</subject><subject>beta-N-Acetylhexosaminidases - chemistry</subject><subject>beta-N-Acetylhexosaminidases - genetics</subject><subject>beta-N-Acetylhexosaminidases - isolation & purification</subject><subject>beta-N-Acetylhexosaminidases - metabolism</subject><subject>Biological and medical sciences</subject><subject>chitooligosaccharides</subject><subject>Chitosan - metabolism</subject><subject>Cloning, Molecular</subject><subject>Enzyme Stability</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Molecular Weight</subject><subject>N‐acetylhexosaminidase</subject><subject>Oligosaccharides - metabolism</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Stenotrophomonas maltophilia</subject><subject>Stenotrophomonas maltophilia - enzymology</subject><subject>Stenotrophomonas maltophilia - genetics</subject><subject>Temperature</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcGOFCEQhonRuOPq2Zvpi4kxYRe6aaCPZuKqyagH9UxoKHYwdDNCtzo-lg_iM8nYs6MHE61LpYrvryryI_SQkgta4pK2gmHecXlB67oRt9Dq1LmNVqQRElPSiTN0L-ePhBBWE34XndVNx1tCxQp9W2_9FGPw1zFrY7Y6eQu50gkqE8fPkCaw1RSrN1gbmPbhOsymkIMfoer3pzb-8R1v4evy4q3OULkUh-rdBGOcUtxt4xBHnatBh6lUPnh9H91xOmR4cMzn6MPV8_frl3jz9sWr9bMNNoxRgXX5hXAcWEul7UhtBYFeOy2ZtaY3wkouS-ZOmlpQ4L3krCGmdYK5nri2OUdPlrm7FD_NkCc1-GwgBD1CnLOijMtGdIT-D8qapqNCsoJeLqhJMecETu2SH3TaK0rUwRt1cEIdnFC_vCmKR8fhcz-APfE3ZhTg8RHQ2ejgkh6Nz785IetaMF64duG--AD7f-1VV683Nwc8XXRx3v1Vhf-49ice4LV-</recordid><startdate>201311</startdate><enddate>201311</enddate><creator>Katta, Suma</creator><creator>Ankati, Sravani</creator><creator>Podile, Appa Rao</creator><general>Blackwell Publishing Ltd</general><general>Wiley-Blackwell</general><scope>IQODW</scope><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><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>201311</creationdate><title>Chitooligosaccharides are converted to N-acetylglucosamine by N-acetyl-β-hexosaminidase from Stenotrophomonas maltophilia</title><author>Katta, Suma ; Ankati, Sravani ; Podile, Appa Rao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4417-a0377f6e4518d902d70ebafa84ddcbc7d868cbc6f8c271e6b86430c5f74fb0f53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Acetylglucosamine - metabolism</topic><topic>Bacteriology</topic><topic>beta-N-Acetylhexosaminidases - chemistry</topic><topic>beta-N-Acetylhexosaminidases - genetics</topic><topic>beta-N-Acetylhexosaminidases - isolation & purification</topic><topic>beta-N-Acetylhexosaminidases - metabolism</topic><topic>Biological and medical sciences</topic><topic>chitooligosaccharides</topic><topic>Chitosan - metabolism</topic><topic>Cloning, Molecular</topic><topic>Enzyme Stability</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Molecular Weight</topic><topic>N‐acetylhexosaminidase</topic><topic>Oligosaccharides - metabolism</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Stenotrophomonas maltophilia</topic><topic>Stenotrophomonas maltophilia - enzymology</topic><topic>Stenotrophomonas maltophilia - genetics</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Katta, Suma</creatorcontrib><creatorcontrib>Ankati, Sravani</creatorcontrib><creatorcontrib>Podile, Appa Rao</creatorcontrib><collection>Pascal-Francis</collection><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><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Katta, Suma</au><au>Ankati, Sravani</au><au>Podile, Appa Rao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chitooligosaccharides are converted to N-acetylglucosamine by N-acetyl-β-hexosaminidase from Stenotrophomonas maltophilia</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2013-11</date><risdate>2013</risdate><volume>348</volume><issue>1</issue><spage>19</spage><epage>25</epage><pages>19-25</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Abstract
The Stenotrophomonas maltophilia k279a (Stm) Hex gene encodes a polypeptide of 785 amino acid residues, with an N-terminal signal peptide. StmHex was cloned without signal peptide and expressed as an 83.6 kDa soluble protein in Escherichia coli BL21 (DE3). Purified StmHex was optimally active at pH 5.0 and 40 °C. The Vmax, Km and kcat/Km for StmHex towards chitin hexamer were 10.55 nkat (mg protein)−1, 271 μM and 0.246 s−1 mM−1, while the kinetic values with chitobiose were 30.65 nkat (mg protein)−1, 2365 μM and 0.082 s−1 mM−1, respectively. Hydrolytic activity on chitooligosaccharides indicated that StmHex was an exo-acting enzyme and yielded N-acetyl-d-glucosamine (GlcNAc) as the final product. StmHex hydrolysed chitooligosaccharides (up to hexamer) into GlcNAc within 60 min, suggesting that this enzyme has potential for use in large-scale production of GlcNAc from chitooligosaccharides.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>23965017</pmid><doi>10.1111/1574-6968.12237</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | FEMS microbiology letters, 2013-11, Vol.348 (1), p.19-25 |
| issn | 0378-1097 1574-6968 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1468379015 |
| source | MEDLINE; Access via Wiley Online Library; Oxford University Press Journals All Titles (1996-Current) |
| subjects | Acetylglucosamine - metabolism Bacteriology beta-N-Acetylhexosaminidases - chemistry beta-N-Acetylhexosaminidases - genetics beta-N-Acetylhexosaminidases - isolation & purification beta-N-Acetylhexosaminidases - metabolism Biological and medical sciences chitooligosaccharides Chitosan - metabolism Cloning, Molecular Enzyme Stability Escherichia coli Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Kinetics Microbiology Miscellaneous Molecular Weight N‐acetylhexosaminidase Oligosaccharides - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Stenotrophomonas maltophilia Stenotrophomonas maltophilia - enzymology Stenotrophomonas maltophilia - genetics Temperature |
| title | Chitooligosaccharides are converted to N-acetylglucosamine by N-acetyl-β-hexosaminidase from Stenotrophomonas maltophilia |
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