Purification and characterization of a novel isozyme of chitinase from Bombyx mori
75-kDa chitinase, which showed potential as a biocontrol agent against Japanese pine sawyer, was characterized after purification from the integument of the fifth instar larvae of Bombyx mori by chromatography on diethylaminoethyl (DEAE)-Toyoperal 650 (M), hydroxylapatite, and Fractogel EMD DEAE 650...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2006-01, Vol.70 (1), p.252-262 |
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| creator | Kabir, K.E,(Yamaguchi Univ. (Japan). Faculty of Agriculture) Hirowatari, D Watanabe, K Koga, D |
| description | 75-kDa chitinase, which showed potential as a biocontrol agent against Japanese pine sawyer, was characterized after purification from the integument of the fifth instar larvae of Bombyx mori by chromatography on diethylaminoethyl (DEAE)-Toyoperal 650 (M), hydroxylapatite, and Fractogel EMD DEAE 650 (M) columns. The optimum pH was 6.0 toward N-acetylchitopentaose (GlcNAcsub(5)) and 10 toward glycolchitin. The optimum temperature was 60 deg C toward GlcNAcsub(5) and 25 deg C toward glycolchitn. The enzyme was stable at pH 7-10 and below 40 deg C. Kinetic analysis and reactionpattern analysis using glycolchitin and N-acetylchitooligosacchraides as substrates indicated that 75-kDa chitinase is an endo- or random-type hydrolytic enzyme to produce the beta anomeric product and that it prefers the longer N-acetylchitooligosacchraides, suggesting, together with the N-terminal amino acid sequence, that the 75-kDa chitinase belongs to family 18 of glycosyl hydrolases. |
| doi_str_mv | 10.1271/bbb.70.252 |
| format | Article |
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(Japan). Faculty of Agriculture) ; Hirowatari, D ; Watanabe, K ; Koga, D</creator><creatorcontrib>Kabir, K.E,(Yamaguchi Univ. (Japan). Faculty of Agriculture) ; Hirowatari, D ; Watanabe, K ; Koga, D</creatorcontrib><description>75-kDa chitinase, which showed potential as a biocontrol agent against Japanese pine sawyer, was characterized after purification from the integument of the fifth instar larvae of Bombyx mori by chromatography on diethylaminoethyl (DEAE)-Toyoperal 650 (M), hydroxylapatite, and Fractogel EMD DEAE 650 (M) columns. The optimum pH was 6.0 toward N-acetylchitopentaose (GlcNAcsub(5)) and 10 toward glycolchitin. The optimum temperature was 60 deg C toward GlcNAcsub(5) and 25 deg C toward glycolchitn. The enzyme was stable at pH 7-10 and below 40 deg C. Kinetic analysis and reactionpattern analysis using glycolchitin and N-acetylchitooligosacchraides as substrates indicated that 75-kDa chitinase is an endo- or random-type hydrolytic enzyme to produce the beta anomeric product and that it prefers the longer N-acetylchitooligosacchraides, suggesting, together with the N-terminal amino acid sequence, that the 75-kDa chitinase belongs to family 18 of glycosyl hydrolases.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.70.252</identifier><identifier>PMID: 16428844</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>Acetylation ; Amino Acid Sequence ; Animals ; Biological and medical sciences ; Bombyx - enzymology ; BOMBYX MORI ; CHEMICOPHYSICAL PROPERTIES ; Chitin - chemistry ; Chitin - metabolism ; CHITINASE ; Chitinases - chemistry ; Chitinases - isolation & purification ; Chitinases - metabolism ; CHROMATOGRAPHIE ; CHROMATOGRAPHY ; Chromatography, High Pressure Liquid ; CROMATOGRAFIA ; Enzyme Stability ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; INSECTICIDAS ; INSECTICIDE ; INSECTICIDES ; Isoenzymes - chemistry ; Isoenzymes - isolation & purification ; Isoenzymes - metabolism ; Kinetics ; Molecular Sequence Data ; Molecular Weight ; properties ; PROPIEDADES FISICOQUIMICAS ; PROPRIETE PHYSICOCHIMIQUE ; PURIFICACION ; PURIFICATION ; QUITINASA ; Substrate Specificity ; Temperature</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2006-01, Vol.70 (1), p.252-262</ispartof><rights>2006 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 2006</rights><rights>2006 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c568t-2a34333253969584ef285dca6f5e52f60fb10bac69a1ba770602b0354ad31c0d3</citedby><cites>FETCH-LOGICAL-c568t-2a34333253969584ef285dca6f5e52f60fb10bac69a1ba770602b0354ad31c0d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17665421$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16428844$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kabir, K.E,(Yamaguchi Univ. (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Hirowatari, D</creatorcontrib><creatorcontrib>Watanabe, K</creatorcontrib><creatorcontrib>Koga, D</creatorcontrib><title>Purification and characterization of a novel isozyme of chitinase from Bombyx mori</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>75-kDa chitinase, which showed potential as a biocontrol agent against Japanese pine sawyer, was characterized after purification from the integument of the fifth instar larvae of Bombyx mori by chromatography on diethylaminoethyl (DEAE)-Toyoperal 650 (M), hydroxylapatite, and Fractogel EMD DEAE 650 (M) columns. The optimum pH was 6.0 toward N-acetylchitopentaose (GlcNAcsub(5)) and 10 toward glycolchitin. The optimum temperature was 60 deg C toward GlcNAcsub(5) and 25 deg C toward glycolchitn. The enzyme was stable at pH 7-10 and below 40 deg C. Kinetic analysis and reactionpattern analysis using glycolchitin and N-acetylchitooligosacchraides as substrates indicated that 75-kDa chitinase is an endo- or random-type hydrolytic enzyme to produce the beta anomeric product and that it prefers the longer N-acetylchitooligosacchraides, suggesting, together with the N-terminal amino acid sequence, that the 75-kDa chitinase belongs to family 18 of glycosyl hydrolases.</description><subject>Acetylation</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Bombyx - enzymology</subject><subject>BOMBYX MORI</subject><subject>CHEMICOPHYSICAL PROPERTIES</subject><subject>Chitin - chemistry</subject><subject>Chitin - metabolism</subject><subject>CHITINASE</subject><subject>Chitinases - chemistry</subject><subject>Chitinases - isolation & purification</subject><subject>Chitinases - metabolism</subject><subject>CHROMATOGRAPHIE</subject><subject>CHROMATOGRAPHY</subject><subject>Chromatography, High Pressure Liquid</subject><subject>CROMATOGRAFIA</subject><subject>Enzyme Stability</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>INSECTICIDAS</subject><subject>INSECTICIDE</subject><subject>INSECTICIDES</subject><subject>Isoenzymes - chemistry</subject><subject>Isoenzymes - isolation & purification</subject><subject>Isoenzymes - metabolism</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>properties</subject><subject>PROPIEDADES FISICOQUIMICAS</subject><subject>PROPRIETE PHYSICOCHIMIQUE</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>QUITINASA</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0k1rFTEUBuAgFnutbtwrA6KLwlzznczSFj8pWETX4SST2JSZSZvMVG9_vSlzpSCCq8DhOSc5vEHoGcFbQhV5Y63dKrylgj5AG8K4amXH1UO0wR2RreaCHKLHpVxiXAuCPEKHRHKqNecb9PV8yTFEB3NMUwNT37gLyOBmn-PtWkyhgWZKN35oYkm3u9HfldxFnOMExTchp7E5SaPd_WrGlOMTdBBgKP7p_jxC39-_-3b6sT378uHT6duz1gmp55YC44wxKlgnO6G5D1SL3oEMwgsaJA6WYAtOdkAsKIUlphYzwaFnxOGeHaHX69yrnK4XX2YzxuL8MMDk01JM7dCSdfi_kCguO6JVhS__gpdpyVNdwhDOO01YRVUdr8rlVEr2wVzlOELeGYLNXSCmBlJvNzWQil_sRy529P093SdQwas9gOJgCBkmF8u9U1IKTkl1YnVxCimP8DPloTcz7IaU_zSxfz7g-doXIBn4kSv7fE4xVhiz-jPYb3C-rLo</recordid><startdate>200601</startdate><enddate>200601</enddate><creator>Kabir, K.E,(Yamaguchi Univ. (Japan). Faculty of Agriculture)</creator><creator>Hirowatari, D</creator><creator>Watanabe, K</creator><creator>Koga, D</creator><general>Japan Society for Bioscience, Biotechnology, and Agrochemistry</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</general><general>Oxford University Press</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>7QO</scope><scope>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>200601</creationdate><title>Purification and characterization of a novel isozyme of chitinase from Bombyx mori</title><author>Kabir, K.E,(Yamaguchi Univ. (Japan). Faculty of Agriculture) ; Hirowatari, D ; Watanabe, K ; Koga, D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c568t-2a34333253969584ef285dca6f5e52f60fb10bac69a1ba770602b0354ad31c0d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Acetylation</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Bombyx - enzymology</topic><topic>BOMBYX MORI</topic><topic>CHEMICOPHYSICAL PROPERTIES</topic><topic>Chitin - chemistry</topic><topic>Chitin - metabolism</topic><topic>CHITINASE</topic><topic>Chitinases - chemistry</topic><topic>Chitinases - isolation & purification</topic><topic>Chitinases - metabolism</topic><topic>CHROMATOGRAPHIE</topic><topic>CHROMATOGRAPHY</topic><topic>Chromatography, High Pressure Liquid</topic><topic>CROMATOGRAFIA</topic><topic>Enzyme Stability</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>INSECTICIDAS</topic><topic>INSECTICIDE</topic><topic>INSECTICIDES</topic><topic>Isoenzymes - chemistry</topic><topic>Isoenzymes - isolation & purification</topic><topic>Isoenzymes - metabolism</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>properties</topic><topic>PROPIEDADES FISICOQUIMICAS</topic><topic>PROPRIETE PHYSICOCHIMIQUE</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>QUITINASA</topic><topic>Substrate Specificity</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kabir, K.E,(Yamaguchi Univ. (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Hirowatari, D</creatorcontrib><creatorcontrib>Watanabe, K</creatorcontrib><creatorcontrib>Koga, D</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>Biotechnology Research Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kabir, K.E,(Yamaguchi Univ. (Japan). Faculty of Agriculture)</au><au>Hirowatari, D</au><au>Watanabe, K</au><au>Koga, D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of a novel isozyme of chitinase from Bombyx mori</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2006-01</date><risdate>2006</risdate><volume>70</volume><issue>1</issue><spage>252</spage><epage>262</epage><pages>252-262</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>75-kDa chitinase, which showed potential as a biocontrol agent against Japanese pine sawyer, was characterized after purification from the integument of the fifth instar larvae of Bombyx mori by chromatography on diethylaminoethyl (DEAE)-Toyoperal 650 (M), hydroxylapatite, and Fractogel EMD DEAE 650 (M) columns. The optimum pH was 6.0 toward N-acetylchitopentaose (GlcNAcsub(5)) and 10 toward glycolchitin. The optimum temperature was 60 deg C toward GlcNAcsub(5) and 25 deg C toward glycolchitn. The enzyme was stable at pH 7-10 and below 40 deg C. Kinetic analysis and reactionpattern analysis using glycolchitin and N-acetylchitooligosacchraides as substrates indicated that 75-kDa chitinase is an endo- or random-type hydrolytic enzyme to produce the beta anomeric product and that it prefers the longer N-acetylchitooligosacchraides, suggesting, together with the N-terminal amino acid sequence, that the 75-kDa chitinase belongs to family 18 of glycosyl hydrolases.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>16428844</pmid><doi>10.1271/bbb.70.252</doi><tpages>11</tpages></addata></record> |
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| identifier | ISSN: 0916-8451 |
| ispartof | Bioscience, biotechnology, and biochemistry, 2006-01, Vol.70 (1), p.252-262 |
| issn | 0916-8451 1347-6947 |
| language | eng |
| recordid | cdi_pubmed_primary_16428844 |
| source | Freely Accessible Japanese Titles (ERDB Project); Oxford University Press Journals All Titles (1996-Current); MEDLINE; J-STAGE日本語サイト (Free Access); Free Full-Text Journals in Chemistry; EZB Electronic Journals Library |
| subjects | Acetylation Amino Acid Sequence Animals Biological and medical sciences Bombyx - enzymology BOMBYX MORI CHEMICOPHYSICAL PROPERTIES Chitin - chemistry Chitin - metabolism CHITINASE Chitinases - chemistry Chitinases - isolation & purification Chitinases - metabolism CHROMATOGRAPHIE CHROMATOGRAPHY Chromatography, High Pressure Liquid CROMATOGRAFIA Enzyme Stability Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration INSECTICIDAS INSECTICIDE INSECTICIDES Isoenzymes - chemistry Isoenzymes - isolation & purification Isoenzymes - metabolism Kinetics Molecular Sequence Data Molecular Weight properties PROPIEDADES FISICOQUIMICAS PROPRIETE PHYSICOCHIMIQUE PURIFICACION PURIFICATION QUITINASA Substrate Specificity Temperature |
| title | Purification and characterization of a novel isozyme of chitinase from Bombyx mori |
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