Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin
A chitin-degrading bacterial strain, KN1699, isolated from Yatsu dry beach (Narashino, Chiba Prefecture, Japan), was identified as Vibrio parahaemolyticus. Treatment of powdered chitin with crude enzyme solution prepared from the supernatant of KN1699 cultures yielded a disaccharide, β-d-N-acetylglu...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2007-05, Vol.75 (2), p.357-365 |
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| creator | Kadokura, K Rokutani, A Yamamoto, M Ikegami, T Sugita, H Itoi, S Hakamata, W Oku, T Nishio, T |
| description | A chitin-degrading bacterial strain, KN1699, isolated from Yatsu dry beach (Narashino, Chiba Prefecture, Japan), was identified as Vibrio parahaemolyticus. Treatment of powdered chitin with crude enzyme solution prepared from the supernatant of KN1699 cultures yielded a disaccharide, β-d-N-acetylglucosaminyl-(1,4)-d-glucosamine (GlcNAc-GlcN), as the primary chitin degradation product. The extracellular enzymes involved in the production of this heterodisaccharide, chitinase (Pa-Chi; molecular mass, 92 kDa) and chitin oligosaccharide deacetylase (Pa-COD; molecular mass, 46 kDa), were isolated from the crude enzyme solution, and their hydrolysis specificities were elucidated. These studies confirmed that (1) Pa-Chi hydrolyzes chitin to produce (GlcNAc)₂ and (2) Pa-COD hydrolyzes the acetamide group of reducing end GlcNAc residue of (GlcNAc)₂. These findings indicate that GlcNAc-GlcN is produced from chitin by the cooperative hydrolytic reactions of both Pa-Chi and Pa-COD. |
| doi_str_mv | 10.1007/s00253-006-0831-6 |
| format | Article |
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Treatment of powdered chitin with crude enzyme solution prepared from the supernatant of KN1699 cultures yielded a disaccharide, β-d-N-acetylglucosaminyl-(1,4)-d-glucosamine (GlcNAc-GlcN), as the primary chitin degradation product. The extracellular enzymes involved in the production of this heterodisaccharide, chitinase (Pa-Chi; molecular mass, 92 kDa) and chitin oligosaccharide deacetylase (Pa-COD; molecular mass, 46 kDa), were isolated from the crude enzyme solution, and their hydrolysis specificities were elucidated. These studies confirmed that (1) Pa-Chi hydrolyzes chitin to produce (GlcNAc)₂ and (2) Pa-COD hydrolyzes the acetamide group of reducing end GlcNAc residue of (GlcNAc)₂. These findings indicate that GlcNAc-GlcN is produced from chitin by the cooperative hydrolytic reactions of both Pa-Chi and Pa-COD.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-006-0831-6</identifier><identifier>PMID: 17334758</identifier><identifier>CODEN: AMBIDG</identifier><language>eng</language><publisher>Berlin: Berlin/Heidelberg : Springer-Verlag</publisher><subject>Acetylglucosamine - biosynthesis ; Acetylglucosamine - chemistry ; Amidohydrolases - chemistry ; Amidohydrolases - isolation & purification ; Amidohydrolases - metabolism ; Amino Acid Sequence ; Bacteria ; Biological and medical sciences ; Biotechnology ; Biotechnology - methods ; Brackish ; Cellular biology ; Chitin ; Chitin - metabolism ; Chitinase ; Chitinases - chemistry ; Chitinases - isolation & purification ; Chitinases - metabolism ; Disaccharides - biosynthesis ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Japan ; Molecular Sequence Data ; Oligosaccharides - metabolism ; Physiology ; Proteins ; Seawater ; Sodium ; Soil Microbiology ; Studies ; Substrate Specificity ; Vibrio parahaemolyticus ; Vibrio parahaemolyticus - classification ; Vibrio parahaemolyticus - enzymology ; Vibrio parahaemolyticus - genetics ; Vibrio parahaemolyticus - isolation & purification</subject><ispartof>Applied microbiology and biotechnology, 2007-05, Vol.75 (2), p.357-365</ispartof><rights>2007 INIST-CNRS</rights><rights>Springer-Verlag 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c477t-cabead3c30dedcf2aa92631ce60d8fb73c4f387377a1faf76b874ffa033565e23</citedby><cites>FETCH-LOGICAL-c477t-cabead3c30dedcf2aa92631ce60d8fb73c4f387377a1faf76b874ffa033565e23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18759527$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17334758$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kadokura, K</creatorcontrib><creatorcontrib>Rokutani, A</creatorcontrib><creatorcontrib>Yamamoto, M</creatorcontrib><creatorcontrib>Ikegami, T</creatorcontrib><creatorcontrib>Sugita, H</creatorcontrib><creatorcontrib>Itoi, S</creatorcontrib><creatorcontrib>Hakamata, W</creatorcontrib><creatorcontrib>Oku, T</creatorcontrib><creatorcontrib>Nishio, T</creatorcontrib><title>Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><description>A chitin-degrading bacterial strain, KN1699, isolated from Yatsu dry beach (Narashino, Chiba Prefecture, Japan), was identified as Vibrio parahaemolyticus. Treatment of powdered chitin with crude enzyme solution prepared from the supernatant of KN1699 cultures yielded a disaccharide, β-d-N-acetylglucosaminyl-(1,4)-d-glucosamine (GlcNAc-GlcN), as the primary chitin degradation product. The extracellular enzymes involved in the production of this heterodisaccharide, chitinase (Pa-Chi; molecular mass, 92 kDa) and chitin oligosaccharide deacetylase (Pa-COD; molecular mass, 46 kDa), were isolated from the crude enzyme solution, and their hydrolysis specificities were elucidated. These studies confirmed that (1) Pa-Chi hydrolyzes chitin to produce (GlcNAc)₂ and (2) Pa-COD hydrolyzes the acetamide group of reducing end GlcNAc residue of (GlcNAc)₂. These findings indicate that GlcNAc-GlcN is produced from chitin by the cooperative hydrolytic reactions of both Pa-Chi and Pa-COD.</description><subject>Acetylglucosamine - biosynthesis</subject><subject>Acetylglucosamine - chemistry</subject><subject>Amidohydrolases - chemistry</subject><subject>Amidohydrolases - isolation & purification</subject><subject>Amidohydrolases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Bacteria</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Biotechnology - methods</subject><subject>Brackish</subject><subject>Cellular biology</subject><subject>Chitin</subject><subject>Chitin - metabolism</subject><subject>Chitinase</subject><subject>Chitinases - chemistry</subject><subject>Chitinases - isolation & purification</subject><subject>Chitinases - metabolism</subject><subject>Disaccharides - biosynthesis</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Japan</subject><subject>Molecular Sequence Data</subject><subject>Oligosaccharides - metabolism</subject><subject>Physiology</subject><subject>Proteins</subject><subject>Seawater</subject><subject>Sodium</subject><subject>Soil Microbiology</subject><subject>Studies</subject><subject>Substrate Specificity</subject><subject>Vibrio parahaemolyticus</subject><subject>Vibrio parahaemolyticus - classification</subject><subject>Vibrio parahaemolyticus - enzymology</subject><subject>Vibrio parahaemolyticus - genetics</subject><subject>Vibrio parahaemolyticus - isolation & purification</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</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>eNqFkstu1DAUhi0EotPCA7CBCKnsAsd2EnuWVUULUiWQoGytE186rpJ4sJOK4cn6eDhKUCs2rHz7zn8uvwl5ReE9BRAfEgCreQnQlCA5LZsnZEMrzkpoaPWUbICKuhT1Vh6R45RuASiTTfOcHFHBeSVquSH3X6fondc4-jAUOJhC7zCiHm30v5fL4Iofvo0-FPv8skPbh-4wej2lwv4aM2u7buow5kg_-gGTXXXmUxE6fxMS6lnWG1sYmwPGQzdjfrgL3Z01eVOMO1vsYzCT_pt0Z3MRwfhHwS6GfhV-QZ457JJ9ua4n5Pri4_fzT-XVl8vP52dXpa6EGEuNrUXDNQdjjXYMccsaTrVtwEjXCq4rx6XgQiB16ETTSlE5h8B53dSW8RPybtHNxf2cbBpV79PcMg42TEkJqEWVx_1fkEFWzPPP4Nt_wNswxSE3oZiUFWOw5RmiC6RjSClap_bR9xgPioKazVeL-Sqbr2bz1Sz8ehWe2t6ah4jV7QycrgAmjZ2LOGifHjiZ_0rNRObeLJzDoPAmZub6GwPKc95txSTwP2IExrw</recordid><startdate>20070501</startdate><enddate>20070501</enddate><creator>Kadokura, K</creator><creator>Rokutani, A</creator><creator>Yamamoto, M</creator><creator>Ikegami, T</creator><creator>Sugita, H</creator><creator>Itoi, S</creator><creator>Hakamata, W</creator><creator>Oku, T</creator><creator>Nishio, T</creator><general>Berlin/Heidelberg : Springer-Verlag</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</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>8FL</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7QO</scope><scope>7TN</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>20070501</creationdate><title>Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin</title><author>Kadokura, K ; Rokutani, A ; Yamamoto, M ; Ikegami, T ; Sugita, H ; Itoi, S ; Hakamata, W ; Oku, T ; Nishio, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c477t-cabead3c30dedcf2aa92631ce60d8fb73c4f387377a1faf76b874ffa033565e23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Acetylglucosamine - biosynthesis</topic><topic>Acetylglucosamine - chemistry</topic><topic>Amidohydrolases - chemistry</topic><topic>Amidohydrolases - isolation & purification</topic><topic>Amidohydrolases - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Bacteria</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Biotechnology - methods</topic><topic>Brackish</topic><topic>Cellular biology</topic><topic>Chitin</topic><topic>Chitin - metabolism</topic><topic>Chitinase</topic><topic>Chitinases - chemistry</topic><topic>Chitinases - isolation & purification</topic><topic>Chitinases - metabolism</topic><topic>Disaccharides - biosynthesis</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Japan</topic><topic>Molecular Sequence Data</topic><topic>Oligosaccharides - metabolism</topic><topic>Physiology</topic><topic>Proteins</topic><topic>Seawater</topic><topic>Sodium</topic><topic>Soil Microbiology</topic><topic>Studies</topic><topic>Substrate Specificity</topic><topic>Vibrio parahaemolyticus</topic><topic>Vibrio parahaemolyticus - classification</topic><topic>Vibrio parahaemolyticus - enzymology</topic><topic>Vibrio parahaemolyticus - genetics</topic><topic>Vibrio parahaemolyticus - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kadokura, K</creatorcontrib><creatorcontrib>Rokutani, A</creatorcontrib><creatorcontrib>Yamamoto, M</creatorcontrib><creatorcontrib>Ikegami, T</creatorcontrib><creatorcontrib>Sugita, H</creatorcontrib><creatorcontrib>Itoi, S</creatorcontrib><creatorcontrib>Hakamata, W</creatorcontrib><creatorcontrib>Oku, T</creatorcontrib><creatorcontrib>Nishio, T</creatorcontrib><collection>AGRIS</collection><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>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Access via ABI/INFORM (ProQuest)</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</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>ABI/INFORM Collection (Alumni Edition)</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>Business Premium Collection</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>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</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>Biotechnology Research Abstracts</collection><collection>Oceanic Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kadokura, K</au><au>Rokutani, A</au><au>Yamamoto, M</au><au>Ikegami, T</au><au>Sugita, H</au><au>Itoi, S</au><au>Hakamata, W</au><au>Oku, T</au><au>Nishio, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin</atitle><jtitle>Applied microbiology and biotechnology</jtitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2007-05-01</date><risdate>2007</risdate><volume>75</volume><issue>2</issue><spage>357</spage><epage>365</epage><pages>357-365</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><coden>AMBIDG</coden><abstract>A chitin-degrading bacterial strain, KN1699, isolated from Yatsu dry beach (Narashino, Chiba Prefecture, Japan), was identified as Vibrio parahaemolyticus. Treatment of powdered chitin with crude enzyme solution prepared from the supernatant of KN1699 cultures yielded a disaccharide, β-d-N-acetylglucosaminyl-(1,4)-d-glucosamine (GlcNAc-GlcN), as the primary chitin degradation product. The extracellular enzymes involved in the production of this heterodisaccharide, chitinase (Pa-Chi; molecular mass, 92 kDa) and chitin oligosaccharide deacetylase (Pa-COD; molecular mass, 46 kDa), were isolated from the crude enzyme solution, and their hydrolysis specificities were elucidated. These studies confirmed that (1) Pa-Chi hydrolyzes chitin to produce (GlcNAc)₂ and (2) Pa-COD hydrolyzes the acetamide group of reducing end GlcNAc residue of (GlcNAc)₂. These findings indicate that GlcNAc-GlcN is produced from chitin by the cooperative hydrolytic reactions of both Pa-Chi and Pa-COD.</abstract><cop>Berlin</cop><pub>Berlin/Heidelberg : Springer-Verlag</pub><pmid>17334758</pmid><doi>10.1007/s00253-006-0831-6</doi><tpages>9</tpages></addata></record> |
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| subjects | Acetylglucosamine - biosynthesis Acetylglucosamine - chemistry Amidohydrolases - chemistry Amidohydrolases - isolation & purification Amidohydrolases - metabolism Amino Acid Sequence Bacteria Biological and medical sciences Biotechnology Biotechnology - methods Brackish Cellular biology Chitin Chitin - metabolism Chitinase Chitinases - chemistry Chitinases - isolation & purification Chitinases - metabolism Disaccharides - biosynthesis Enzymes Fundamental and applied biological sciences. Psychology Japan Molecular Sequence Data Oligosaccharides - metabolism Physiology Proteins Seawater Sodium Soil Microbiology Studies Substrate Specificity Vibrio parahaemolyticus Vibrio parahaemolyticus - classification Vibrio parahaemolyticus - enzymology Vibrio parahaemolyticus - genetics Vibrio parahaemolyticus - isolation & purification |
| title | Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin |
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