Purification of Amylases and Other Enzymes by a Forced-affinity Chromatography Method
An affinity matrix of soluble starch gel was prepared by cross-linking catalyzed by epichlorohydrin. The elution pattern of Taka-amylase A (TAA) indicated that the amount of enzyme bound to the starch gel column increased with increases in the ammonium sulfate (AmS) concentration in the equilibratin...
Gespeichert in:
| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1997, Vol.61 (5), p.813-816 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 816 |
|---|---|
| container_issue | 5 |
| container_start_page | 813 |
| container_title | Bioscience, biotechnology, and biochemistry |
| container_volume | 61 |
| creator | Kobayashi, Mikihiko Sasaki, Yutaka Kobayashi, Shoichi |
| description | An affinity matrix of soluble starch gel was prepared by cross-linking catalyzed by epichlorohydrin. The elution pattern of Taka-amylase A (TAA) indicated that the amount of enzyme bound to the starch gel column increased with increases in the ammonium sulfate (AmS) concentration in the equilibrating buffer. TAA had an affinity for the gels with a starch structure, and desorbed from the column with the buffer containing no AmS. Bound TAA was also eluted with starch and cyclodextrin solution. The AmS stimulative effect was partially replaced by polyethylene glycol and surfactants. Besides TAA, various other amylases bound satisfactorily to the starch gel. Moreover, affinity purifications of dextranase, cellulase, and pectinase were done by gels with dextran, cellulose, and pectin structures, respectively. By the aid of forced effects of AmS, various carbohydrases could be purified by the affinity gels of polysaccharide linked by epichlorohydrin. |
| doi_str_mv | 10.1271/bbb.61.813 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pasca</sourceid><recordid>TN_cdi_pascalfrancis_primary_2768567</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>79054346</sourcerecordid><originalsourceid>FETCH-LOGICAL-c613t-fc83a244903c78002b8235b6c4fb0d648807ff7d03244b54a67a6af61139d21f3</originalsourceid><addsrcrecordid>eNpt0M9rFDEUB_AgSt1WL96FgOJBmDWZ_JxjWdoqVOrBnsNLJnFTZiZrMoOMf70pu_YgngLvffLe44vQG0q2tFX0k7V2K-lWU_YMbSjjqpEdV8_RhnRUNpoL-hKdl_JASC0IeobOOqq0EGqD7r8tOYboYI5pwingy3EdoPiCYerx3bz3GV9Nv9exVuyKAV-n7HzfQAhxivOKd_ucRpjTjwyH_Yq_-nmf-lfoRYCh-Nen9wLdX199331ubu9uvuwubxsnKZub4DSDlvOOMKc0Ia3VLRNWOh4s6SXXmqgQVE9YRVZwkAokBEkp6_qWBnaBPhznHnL6ufgymzEW54cBJp-WYlRHBGdcVvjuH_iQljzV2wyt-3krWsKr-nhULqdSsg_mkOMIeTWUmMekTU3aSGpq0hW_PY1c7Oj7J3qKtvbfn_pQHAwhw-RieWKtklrIRyaOLE4h5RF-pTz0ZoZ1SPnvH_af9X8ANc2WnQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1449425204</pqid></control><display><type>article</type><title>Purification of Amylases and Other Enzymes by a Forced-affinity Chromatography Method</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Oxford University Press Journals All Titles (1996-Current)</source><source>J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese</source><source>Open Access Titles of Japan</source><source>Free Full-Text Journals in Chemistry</source><creator>Kobayashi, Mikihiko ; Sasaki, Yutaka ; Kobayashi, Shoichi</creator><creatorcontrib>Kobayashi, Mikihiko ; Sasaki, Yutaka ; Kobayashi, Shoichi</creatorcontrib><description>An affinity matrix of soluble starch gel was prepared by cross-linking catalyzed by epichlorohydrin. The elution pattern of Taka-amylase A (TAA) indicated that the amount of enzyme bound to the starch gel column increased with increases in the ammonium sulfate (AmS) concentration in the equilibrating buffer. TAA had an affinity for the gels with a starch structure, and desorbed from the column with the buffer containing no AmS. Bound TAA was also eluted with starch and cyclodextrin solution. The AmS stimulative effect was partially replaced by polyethylene glycol and surfactants. Besides TAA, various other amylases bound satisfactorily to the starch gel. Moreover, affinity purifications of dextranase, cellulase, and pectinase were done by gels with dextran, cellulose, and pectin structures, respectively. By the aid of forced effects of AmS, various carbohydrases could be purified by the affinity gels of polysaccharide linked by epichlorohydrin.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.61.813</identifier><identifier>PMID: 9178557</identifier><language>eng</language><publisher>Tokyo: Taylor & Francis</publisher><subject>Adsorption ; affinity chromatography ; Ammonium Sulfate ; amylases ; Amylases - isolation & purification ; Biological and medical sciences ; Biotechnology ; Chromatography, Affinity - methods ; Cross-Linking Reagents ; Enzyme engineering ; Epichlorohydrin ; forced-affinity chromatography ; Fundamental and applied biological sciences. Psychology ; Gels ; glucanases ; Glycoside Hydrolases - isolation & purification ; Improved methods for extraction and purification of enzymes ; Ligands ; Methods. Procedures. Technologies ; Solubility</subject><ispartof>Bioscience, biotechnology, and biochemistry, 1997, Vol.61 (5), p.813-816</ispartof><rights>Copyright 1997 Taylor and Francis Group LLC 1997</rights><rights>1997 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 1997</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c613t-fc83a244903c78002b8235b6c4fb0d648807ff7d03244b54a67a6af61139d21f3</citedby></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=2768567$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9178557$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kobayashi, Mikihiko</creatorcontrib><creatorcontrib>Sasaki, Yutaka</creatorcontrib><creatorcontrib>Kobayashi, Shoichi</creatorcontrib><title>Purification of Amylases and Other Enzymes by a Forced-affinity Chromatography Method</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>An affinity matrix of soluble starch gel was prepared by cross-linking catalyzed by epichlorohydrin. The elution pattern of Taka-amylase A (TAA) indicated that the amount of enzyme bound to the starch gel column increased with increases in the ammonium sulfate (AmS) concentration in the equilibrating buffer. TAA had an affinity for the gels with a starch structure, and desorbed from the column with the buffer containing no AmS. Bound TAA was also eluted with starch and cyclodextrin solution. The AmS stimulative effect was partially replaced by polyethylene glycol and surfactants. Besides TAA, various other amylases bound satisfactorily to the starch gel. Moreover, affinity purifications of dextranase, cellulase, and pectinase were done by gels with dextran, cellulose, and pectin structures, respectively. By the aid of forced effects of AmS, various carbohydrases could be purified by the affinity gels of polysaccharide linked by epichlorohydrin.</description><subject>Adsorption</subject><subject>affinity chromatography</subject><subject>Ammonium Sulfate</subject><subject>amylases</subject><subject>Amylases - isolation & purification</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Chromatography, Affinity - methods</subject><subject>Cross-Linking Reagents</subject><subject>Enzyme engineering</subject><subject>Epichlorohydrin</subject><subject>forced-affinity chromatography</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>glucanases</subject><subject>Glycoside Hydrolases - isolation & purification</subject><subject>Improved methods for extraction and purification of enzymes</subject><subject>Ligands</subject><subject>Methods. Procedures. Technologies</subject><subject>Solubility</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0M9rFDEUB_AgSt1WL96FgOJBmDWZ_JxjWdoqVOrBnsNLJnFTZiZrMoOMf70pu_YgngLvffLe44vQG0q2tFX0k7V2K-lWU_YMbSjjqpEdV8_RhnRUNpoL-hKdl_JASC0IeobOOqq0EGqD7r8tOYboYI5pwingy3EdoPiCYerx3bz3GV9Nv9exVuyKAV-n7HzfQAhxivOKd_ucRpjTjwyH_Yq_-nmf-lfoRYCh-Nen9wLdX199331ubu9uvuwubxsnKZub4DSDlvOOMKc0Ia3VLRNWOh4s6SXXmqgQVE9YRVZwkAokBEkp6_qWBnaBPhznHnL6ufgymzEW54cBJp-WYlRHBGdcVvjuH_iQljzV2wyt-3krWsKr-nhULqdSsg_mkOMIeTWUmMekTU3aSGpq0hW_PY1c7Oj7J3qKtvbfn_pQHAwhw-RieWKtklrIRyaOLE4h5RF-pTz0ZoZ1SPnvH_af9X8ANc2WnQ</recordid><startdate>1997</startdate><enddate>1997</enddate><creator>Kobayashi, Mikihiko</creator><creator>Sasaki, Yutaka</creator><creator>Kobayashi, Shoichi</creator><general>Taylor & Francis</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</general><general>Oxford University Press</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></search><sort><creationdate>1997</creationdate><title>Purification of Amylases and Other Enzymes by a Forced-affinity Chromatography Method</title><author>Kobayashi, Mikihiko ; Sasaki, Yutaka ; Kobayashi, Shoichi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c613t-fc83a244903c78002b8235b6c4fb0d648807ff7d03244b54a67a6af61139d21f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Adsorption</topic><topic>affinity chromatography</topic><topic>Ammonium Sulfate</topic><topic>amylases</topic><topic>Amylases - isolation & purification</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Chromatography, Affinity - methods</topic><topic>Cross-Linking Reagents</topic><topic>Enzyme engineering</topic><topic>Epichlorohydrin</topic><topic>forced-affinity chromatography</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>glucanases</topic><topic>Glycoside Hydrolases - isolation & purification</topic><topic>Improved methods for extraction and purification of enzymes</topic><topic>Ligands</topic><topic>Methods. Procedures. Technologies</topic><topic>Solubility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kobayashi, Mikihiko</creatorcontrib><creatorcontrib>Sasaki, Yutaka</creatorcontrib><creatorcontrib>Kobayashi, Shoichi</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><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kobayashi, Mikihiko</au><au>Sasaki, Yutaka</au><au>Kobayashi, Shoichi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification of Amylases and Other Enzymes by a Forced-affinity Chromatography Method</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>1997</date><risdate>1997</risdate><volume>61</volume><issue>5</issue><spage>813</spage><epage>816</epage><pages>813-816</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>An affinity matrix of soluble starch gel was prepared by cross-linking catalyzed by epichlorohydrin. The elution pattern of Taka-amylase A (TAA) indicated that the amount of enzyme bound to the starch gel column increased with increases in the ammonium sulfate (AmS) concentration in the equilibrating buffer. TAA had an affinity for the gels with a starch structure, and desorbed from the column with the buffer containing no AmS. Bound TAA was also eluted with starch and cyclodextrin solution. The AmS stimulative effect was partially replaced by polyethylene glycol and surfactants. Besides TAA, various other amylases bound satisfactorily to the starch gel. Moreover, affinity purifications of dextranase, cellulase, and pectinase were done by gels with dextran, cellulose, and pectin structures, respectively. By the aid of forced effects of AmS, various carbohydrases could be purified by the affinity gels of polysaccharide linked by epichlorohydrin.</abstract><cop>Tokyo</cop><pub>Taylor & Francis</pub><pmid>9178557</pmid><doi>10.1271/bbb.61.813</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0916-8451 |
| ispartof | Bioscience, biotechnology, and biochemistry, 1997, Vol.61 (5), p.813-816 |
| issn | 0916-8451 1347-6947 |
| language | eng |
| recordid | cdi_pascalfrancis_primary_2768567 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Oxford University Press Journals All Titles (1996-Current); J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Open Access Titles of Japan; Free Full-Text Journals in Chemistry |
| subjects | Adsorption affinity chromatography Ammonium Sulfate amylases Amylases - isolation & purification Biological and medical sciences Biotechnology Chromatography, Affinity - methods Cross-Linking Reagents Enzyme engineering Epichlorohydrin forced-affinity chromatography Fundamental and applied biological sciences. Psychology Gels glucanases Glycoside Hydrolases - isolation & purification Improved methods for extraction and purification of enzymes Ligands Methods. Procedures. Technologies Solubility |
| title | Purification of Amylases and Other Enzymes by a Forced-affinity Chromatography Method |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T17%3A31%3A02IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pasca&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Purification%20of%20Amylases%20and%20Other%20Enzymes%20by%20a%20Forced-affinity%20Chromatography%20Method&rft.jtitle=Bioscience,%20biotechnology,%20and%20biochemistry&rft.au=Kobayashi,%20Mikihiko&rft.date=1997&rft.volume=61&rft.issue=5&rft.spage=813&rft.epage=816&rft.pages=813-816&rft.issn=0916-8451&rft.eissn=1347-6947&rft_id=info:doi/10.1271/bbb.61.813&rft_dat=%3Cproquest_pasca%3E79054346%3C/proquest_pasca%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1449425204&rft_id=info:pmid/9178557&rfr_iscdi=true |