Purification and Characterization of Chitin Deacetylase from Colletotrichum lindemuthianum(∗)
Chitin deacetylase (EC 3.5.1.41), the enzyme that catalyzes the hydrolysis of acetamido groups of N-acetyl-D-glucosamine in chitin, has been purified to homogeneity from the culture filtrate of the fungus Colletotrichum lindemuthianum and further characterized. The enzyme is a glycoprotein, and its...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 1995-11, Vol.270 (44), p.26286-26291 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 26291 |
|---|---|
| container_issue | 44 |
| container_start_page | 26286 |
| container_title | The Journal of biological chemistry |
| container_volume | 270 |
| creator | Tsigos, Iason Bouriotis, Vassilis |
| description | Chitin deacetylase (EC 3.5.1.41), the enzyme that catalyzes the hydrolysis of acetamido groups of N-acetyl-D-glucosamine in chitin, has been purified to homogeneity from the culture filtrate of the fungus Colletotrichum lindemuthianum and further characterized. The enzyme is a glycoprotein, and its apparent molecular mass was determined to be ~150 kDa. The glycosylation pattern of the enzyme is consistent with a mixture of N-linked glycans including oligomannosidic hybrid and/or complex type, and its carbohydrate content is approximately 67% by weight. Chitin deacetylase is active on several chitinous substrates and chitin derivatives, is not considerably inhibited by carboxylic acids, especially acetic acid, and exhibits a remarkable thermostability. The enzyme requires at least two N-acetyl-D-glucosamine residues (chitobiose) for catalysis. When glycol chitin (a water-soluble chitin derivative) was used as substrate, the optimum temperature for enzyme activity was determined to be 50°C, and the optimum pH was ~8.5. |
| doi_str_mv | 10.1074/jbc.270.44.26286 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_77653960</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925818924762</els_id><sourcerecordid>77653960</sourcerecordid><originalsourceid>FETCH-LOGICAL-c532t-8c019384d6860a2a5f78c3a0ec9ae8f22378f027ac01389c17f7aaa0c5a6f76d3</originalsourceid><addsrcrecordid>eNqFkE2L1TAUhoMo43V0L4LQhYgues1Hm6Tu5PoJAwo64C6cm55MM7TNmKQzjL_Af-D_85cY7cWFIGYTOO9z3oSHkPuMbhlVzbPzvd1yRbdNs-WSa3mDbBjVohYt-3yTbCjlrO54q2-TOymd03Kajh2RI9V2XAu9IebDEr3zFrIPcwVzX-0GiGAzRv91HQZXZj77uXqJYDFfj5CwcjFM1S6MI-aQo7fDMlWjn3ucljx4mJfpyY9v35_eJbccjAnvHe5jcvr61afd2_rk_Zt3uxcntW0Fz7W2lHVCN73UkgKH1iltBVC0HaB2nAulHeUKCid0Z5lyCgCobUE6JXtxTB6vvRcxfFkwZTP5ZHEcYcawJKOUbEUn6X9Bpigtj8kC0hW0MaQU0ZmL6CeI14ZR80u-KfJNkW-axvyWX1YeHrqX_YT9n4WD7ZI_WvPBnw1XPqLZ-2AHnP6uebBiDoKBs-iTOf3YKaZaIUr4fA2x2Lz0GE2yHmeLfemz2fTB__uDPwF-qalo</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17003786</pqid></control><display><type>article</type><title>Purification and Characterization of Chitin Deacetylase from Colletotrichum lindemuthianum(∗)</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Tsigos, Iason ; Bouriotis, Vassilis</creator><creatorcontrib>Tsigos, Iason ; Bouriotis, Vassilis</creatorcontrib><description>Chitin deacetylase (EC 3.5.1.41), the enzyme that catalyzes the hydrolysis of acetamido groups of N-acetyl-D-glucosamine in chitin, has been purified to homogeneity from the culture filtrate of the fungus Colletotrichum lindemuthianum and further characterized. The enzyme is a glycoprotein, and its apparent molecular mass was determined to be ~150 kDa. The glycosylation pattern of the enzyme is consistent with a mixture of N-linked glycans including oligomannosidic hybrid and/or complex type, and its carbohydrate content is approximately 67% by weight. Chitin deacetylase is active on several chitinous substrates and chitin derivatives, is not considerably inhibited by carboxylic acids, especially acetic acid, and exhibits a remarkable thermostability. The enzyme requires at least two N-acetyl-D-glucosamine residues (chitobiose) for catalysis. When glycol chitin (a water-soluble chitin derivative) was used as substrate, the optimum temperature for enzyme activity was determined to be 50°C, and the optimum pH was ~8.5.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.270.44.26286</identifier><identifier>PMID: 7592838</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>ACIDE AMINE ; ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; AMIDE HYDROLASE ; AMIDO HIDROLASA ; Amidohydrolases - chemistry ; Amidohydrolases - isolation & purification ; Amidohydrolases - metabolism ; Amino Acids - analysis ; AMINOACIDOS ; Animals ; Brachyura ; Carbohydrates - analysis ; Chitin - metabolism ; CHITINE ; Chromatography, Gel ; Chromatography, Ion Exchange ; COLLETOTRICHUM LINDEMUTHIANUM ; Decapoda ; Electrophoresis, Polyacrylamide Gel ; Enzyme Stability ; Fungi - enzymology ; Kinetics ; MEDIO DE CULTIVO ; MILIEU DE CULTURE ; Monosaccharides - metabolism ; Oligosaccharides - metabolism ; PURIFICACION ; PURIFICATION ; QUITINA ; Substrate Specificity ; TEMPERATURA ; TEMPERATURE</subject><ispartof>The Journal of biological chemistry, 1995-11, Vol.270 (44), p.26286-26291</ispartof><rights>1995 © 1995 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c532t-8c019384d6860a2a5f78c3a0ec9ae8f22378f027ac01389c17f7aaa0c5a6f76d3</citedby><cites>FETCH-LOGICAL-c532t-8c019384d6860a2a5f78c3a0ec9ae8f22378f027ac01389c17f7aaa0c5a6f76d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7592838$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tsigos, Iason</creatorcontrib><creatorcontrib>Bouriotis, Vassilis</creatorcontrib><title>Purification and Characterization of Chitin Deacetylase from Colletotrichum lindemuthianum(∗)</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Chitin deacetylase (EC 3.5.1.41), the enzyme that catalyzes the hydrolysis of acetamido groups of N-acetyl-D-glucosamine in chitin, has been purified to homogeneity from the culture filtrate of the fungus Colletotrichum lindemuthianum and further characterized. The enzyme is a glycoprotein, and its apparent molecular mass was determined to be ~150 kDa. The glycosylation pattern of the enzyme is consistent with a mixture of N-linked glycans including oligomannosidic hybrid and/or complex type, and its carbohydrate content is approximately 67% by weight. Chitin deacetylase is active on several chitinous substrates and chitin derivatives, is not considerably inhibited by carboxylic acids, especially acetic acid, and exhibits a remarkable thermostability. The enzyme requires at least two N-acetyl-D-glucosamine residues (chitobiose) for catalysis. When glycol chitin (a water-soluble chitin derivative) was used as substrate, the optimum temperature for enzyme activity was determined to be 50°C, and the optimum pH was ~8.5.</description><subject>ACIDE AMINE</subject><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>AMIDE HYDROLASE</subject><subject>AMIDO HIDROLASA</subject><subject>Amidohydrolases - chemistry</subject><subject>Amidohydrolases - isolation & purification</subject><subject>Amidohydrolases - metabolism</subject><subject>Amino Acids - analysis</subject><subject>AMINOACIDOS</subject><subject>Animals</subject><subject>Brachyura</subject><subject>Carbohydrates - analysis</subject><subject>Chitin - metabolism</subject><subject>CHITINE</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>COLLETOTRICHUM LINDEMUTHIANUM</subject><subject>Decapoda</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Stability</subject><subject>Fungi - enzymology</subject><subject>Kinetics</subject><subject>MEDIO DE CULTIVO</subject><subject>MILIEU DE CULTURE</subject><subject>Monosaccharides - metabolism</subject><subject>Oligosaccharides - metabolism</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>QUITINA</subject><subject>Substrate Specificity</subject><subject>TEMPERATURA</subject><subject>TEMPERATURE</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE2L1TAUhoMo43V0L4LQhYgues1Hm6Tu5PoJAwo64C6cm55MM7TNmKQzjL_Af-D_85cY7cWFIGYTOO9z3oSHkPuMbhlVzbPzvd1yRbdNs-WSa3mDbBjVohYt-3yTbCjlrO54q2-TOymd03Kajh2RI9V2XAu9IebDEr3zFrIPcwVzX-0GiGAzRv91HQZXZj77uXqJYDFfj5CwcjFM1S6MI-aQo7fDMlWjn3ucljx4mJfpyY9v35_eJbccjAnvHe5jcvr61afd2_rk_Zt3uxcntW0Fz7W2lHVCN73UkgKH1iltBVC0HaB2nAulHeUKCid0Z5lyCgCobUE6JXtxTB6vvRcxfFkwZTP5ZHEcYcawJKOUbEUn6X9Bpigtj8kC0hW0MaQU0ZmL6CeI14ZR80u-KfJNkW-axvyWX1YeHrqX_YT9n4WD7ZI_WvPBnw1XPqLZ-2AHnP6uebBiDoKBs-iTOf3YKaZaIUr4fA2x2Lz0GE2yHmeLfemz2fTB__uDPwF-qalo</recordid><startdate>19951103</startdate><enddate>19951103</enddate><creator>Tsigos, Iason</creator><creator>Bouriotis, Vassilis</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19951103</creationdate><title>Purification and Characterization of Chitin Deacetylase from Colletotrichum lindemuthianum(∗)</title><author>Tsigos, Iason ; Bouriotis, Vassilis</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c532t-8c019384d6860a2a5f78c3a0ec9ae8f22378f027ac01389c17f7aaa0c5a6f76d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>ACIDE AMINE</topic><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>AMIDE HYDROLASE</topic><topic>AMIDO HIDROLASA</topic><topic>Amidohydrolases - chemistry</topic><topic>Amidohydrolases - isolation & purification</topic><topic>Amidohydrolases - metabolism</topic><topic>Amino Acids - analysis</topic><topic>AMINOACIDOS</topic><topic>Animals</topic><topic>Brachyura</topic><topic>Carbohydrates - analysis</topic><topic>Chitin - metabolism</topic><topic>CHITINE</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Ion Exchange</topic><topic>COLLETOTRICHUM LINDEMUTHIANUM</topic><topic>Decapoda</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Stability</topic><topic>Fungi - enzymology</topic><topic>Kinetics</topic><topic>MEDIO DE CULTIVO</topic><topic>MILIEU DE CULTURE</topic><topic>Monosaccharides - metabolism</topic><topic>Oligosaccharides - metabolism</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>QUITINA</topic><topic>Substrate Specificity</topic><topic>TEMPERATURA</topic><topic>TEMPERATURE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tsigos, Iason</creatorcontrib><creatorcontrib>Bouriotis, Vassilis</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tsigos, Iason</au><au>Bouriotis, Vassilis</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Characterization of Chitin Deacetylase from Colletotrichum lindemuthianum(∗)</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1995-11-03</date><risdate>1995</risdate><volume>270</volume><issue>44</issue><spage>26286</spage><epage>26291</epage><pages>26286-26291</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Chitin deacetylase (EC 3.5.1.41), the enzyme that catalyzes the hydrolysis of acetamido groups of N-acetyl-D-glucosamine in chitin, has been purified to homogeneity from the culture filtrate of the fungus Colletotrichum lindemuthianum and further characterized. The enzyme is a glycoprotein, and its apparent molecular mass was determined to be ~150 kDa. The glycosylation pattern of the enzyme is consistent with a mixture of N-linked glycans including oligomannosidic hybrid and/or complex type, and its carbohydrate content is approximately 67% by weight. Chitin deacetylase is active on several chitinous substrates and chitin derivatives, is not considerably inhibited by carboxylic acids, especially acetic acid, and exhibits a remarkable thermostability. The enzyme requires at least two N-acetyl-D-glucosamine residues (chitobiose) for catalysis. When glycol chitin (a water-soluble chitin derivative) was used as substrate, the optimum temperature for enzyme activity was determined to be 50°C, and the optimum pH was ~8.5.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7592838</pmid><doi>10.1074/jbc.270.44.26286</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1995-11, Vol.270 (44), p.26286-26291 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77653960 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | ACIDE AMINE ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE AMIDE HYDROLASE AMIDO HIDROLASA Amidohydrolases - chemistry Amidohydrolases - isolation & purification Amidohydrolases - metabolism Amino Acids - analysis AMINOACIDOS Animals Brachyura Carbohydrates - analysis Chitin - metabolism CHITINE Chromatography, Gel Chromatography, Ion Exchange COLLETOTRICHUM LINDEMUTHIANUM Decapoda Electrophoresis, Polyacrylamide Gel Enzyme Stability Fungi - enzymology Kinetics MEDIO DE CULTIVO MILIEU DE CULTURE Monosaccharides - metabolism Oligosaccharides - metabolism PURIFICACION PURIFICATION QUITINA Substrate Specificity TEMPERATURA TEMPERATURE |
| title | Purification and Characterization of Chitin Deacetylase from Colletotrichum lindemuthianum(∗) |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-20T02%3A08%3A26IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Purification%20and%20Characterization%20of%20Chitin%20Deacetylase%20from%20Colletotrichum%20lindemuthianum(%E2%88%97)&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Tsigos,%20Iason&rft.date=1995-11-03&rft.volume=270&rft.issue=44&rft.spage=26286&rft.epage=26291&rft.pages=26286-26291&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.270.44.26286&rft_dat=%3Cproquest_cross%3E77653960%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17003786&rft_id=info:pmid/7592838&rft_els_id=S0021925818924762&rfr_iscdi=true |