Purification by expanded bed adsorption and characterization of an α-amylases FORILASE NTL ® from A. niger
In this work the purification and biochemistry characterization of α-amylases from Aspergillus niger (FORILASE NTL ®) were studied. The effects of expansion degree of resin bed on enzyme purification by expanded bed adsorption (EBA) have also been studied. Residence time distributions (RTD) studies...
Gespeichert in:
| Veröffentlicht in: | Journal of chromatography. B, Analytical technologies in the biomedical and life sciences Analytical technologies in the biomedical and life sciences, 2007-02, Vol.846 (1), p.51-56 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 56 |
|---|---|
| container_issue | 1 |
| container_start_page | 51 |
| container_title | Journal of chromatography. B, Analytical technologies in the biomedical and life sciences |
| container_volume | 846 |
| creator | Toledo, A.L. Severo, J.B. Souza, R.R. Campos, E.S. Santana, J.C.C. Tambourgi, E.B. |
| description | In this work the purification and biochemistry characterization of α-amylases from
Aspergillus niger (FORILASE NTL
®) were studied. The effects of expansion degree of resin bed on enzyme purification by expanded bed adsorption (EBA) have also been studied. Residence time distributions (RTD) studies were done to achieve the optimal conditions of the amylases recovery on ion-exchange resin, and glucose solution was used as a new tracer. Results showed that height equivalent of the theoretical plates (HETP), axial dispersion and the Prandt number increased with bed height, bed voidage and linear velocity. The adsorption capacity of α-amylases, on the resin, increased with bed height and the best condition was at four-expansion degree. α-Amylase characterization showed that this enzyme has high affinity with soluble starch, good hydrolysis potential and molecular weight of 116
kDa. |
| doi_str_mv | 10.1016/j.jchromb.2006.08.011 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68953031</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1570023206006647</els_id><sourcerecordid>68953031</sourcerecordid><originalsourceid>FETCH-LOGICAL-c393t-30f86dc53c2b78f20da87e35a5c7d864b5a9cc8aed9c78ceb1f634724305c41d3</originalsourceid><addsrcrecordid>eNqFkMuKFDEUhoMozkUfQcnG2VWZVCqV1EqaYUYHGkd0BHchdXLipKlLm1SL7UMN-Ao-gM9kxi6YpYuQ8Oc7Fz5CXnBWcsab15tyA7dxGrqyYqwpmS4Z54_IMddKFEI1Xx7nt1SsYJWojshJShvGuGJKPCVHvGllK6U4Jv2HXQw-gJ3DNNJuT_HH1o4OHe3ysS5NcfvvK4cUbm20MGMMPw_85HNO__wq7LDvbcJEL68_Xq1Xny7o-5s1_X1HfV6Rrko6hq8Yn5En3vYJny_3Kfl8eXFz_q5YX7-9Ol-tCxCtmAvBvG4cSAFVp7SvmLNaoZBWgnK6qTtpWwBt0bWgNGDHfSNqVdWCSai5E6fk7NB3G6dvO0yzGUIC7Hs74rRLptGtFEzwDMoDCHFKKaI32xgGG_eGM3Ov2WzMotncazZMm6w5171cBuy6Ad1D1eI1A68WwCawvY92hJAeOF3rltU6c28OHGYd3wNGkyDgCOhCRJiNm8J_VvkLCtufUA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>68953031</pqid></control><display><type>article</type><title>Purification by expanded bed adsorption and characterization of an α-amylases FORILASE NTL ® from A. niger</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Toledo, A.L. ; Severo, J.B. ; Souza, R.R. ; Campos, E.S. ; Santana, J.C.C. ; Tambourgi, E.B.</creator><creatorcontrib>Toledo, A.L. ; Severo, J.B. ; Souza, R.R. ; Campos, E.S. ; Santana, J.C.C. ; Tambourgi, E.B.</creatorcontrib><description>In this work the purification and biochemistry characterization of α-amylases from
Aspergillus niger (FORILASE NTL
®) were studied. The effects of expansion degree of resin bed on enzyme purification by expanded bed adsorption (EBA) have also been studied. Residence time distributions (RTD) studies were done to achieve the optimal conditions of the amylases recovery on ion-exchange resin, and glucose solution was used as a new tracer. Results showed that height equivalent of the theoretical plates (HETP), axial dispersion and the Prandt number increased with bed height, bed voidage and linear velocity. The adsorption capacity of α-amylases, on the resin, increased with bed height and the best condition was at four-expansion degree. α-Amylase characterization showed that this enzyme has high affinity with soluble starch, good hydrolysis potential and molecular weight of 116
kDa.</description><identifier>ISSN: 1570-0232</identifier><identifier>EISSN: 1873-376X</identifier><identifier>DOI: 10.1016/j.jchromb.2006.08.011</identifier><identifier>PMID: 16959553</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Adsorption ; alpha-Amylases - chemistry ; alpha-Amylases - metabolism ; Analysis ; Analytical, structural and metabolic biochemistry ; Aspergillus niger ; Aspergillus niger - enzymology ; Biochemistry characterization ; Biological and medical sciences ; Electrophoresis, Polyacrylamide Gel ; Expanded bed adsorption ; Expansion degree ; Fundamental and applied biological sciences. Psychology ; General pharmacology ; Hydrolysis ; Medical sciences ; Molecular Weight ; Pharmacology. Drug treatments ; Purification ; α-Amylase</subject><ispartof>Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 2007-02, Vol.846 (1), p.51-56</ispartof><rights>2006 Elsevier B.V.</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c393t-30f86dc53c2b78f20da87e35a5c7d864b5a9cc8aed9c78ceb1f634724305c41d3</citedby><cites>FETCH-LOGICAL-c393t-30f86dc53c2b78f20da87e35a5c7d864b5a9cc8aed9c78ceb1f634724305c41d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1570023206006647$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18489048$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16959553$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Toledo, A.L.</creatorcontrib><creatorcontrib>Severo, J.B.</creatorcontrib><creatorcontrib>Souza, R.R.</creatorcontrib><creatorcontrib>Campos, E.S.</creatorcontrib><creatorcontrib>Santana, J.C.C.</creatorcontrib><creatorcontrib>Tambourgi, E.B.</creatorcontrib><title>Purification by expanded bed adsorption and characterization of an α-amylases FORILASE NTL ® from A. niger</title><title>Journal of chromatography. B, Analytical technologies in the biomedical and life sciences</title><addtitle>J Chromatogr B Analyt Technol Biomed Life Sci</addtitle><description>In this work the purification and biochemistry characterization of α-amylases from
Aspergillus niger (FORILASE NTL
®) were studied. The effects of expansion degree of resin bed on enzyme purification by expanded bed adsorption (EBA) have also been studied. Residence time distributions (RTD) studies were done to achieve the optimal conditions of the amylases recovery on ion-exchange resin, and glucose solution was used as a new tracer. Results showed that height equivalent of the theoretical plates (HETP), axial dispersion and the Prandt number increased with bed height, bed voidage and linear velocity. The adsorption capacity of α-amylases, on the resin, increased with bed height and the best condition was at four-expansion degree. α-Amylase characterization showed that this enzyme has high affinity with soluble starch, good hydrolysis potential and molecular weight of 116
kDa.</description><subject>Adsorption</subject><subject>alpha-Amylases - chemistry</subject><subject>alpha-Amylases - metabolism</subject><subject>Analysis</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Aspergillus niger</subject><subject>Aspergillus niger - enzymology</subject><subject>Biochemistry characterization</subject><subject>Biological and medical sciences</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Expanded bed adsorption</subject><subject>Expansion degree</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General pharmacology</subject><subject>Hydrolysis</subject><subject>Medical sciences</subject><subject>Molecular Weight</subject><subject>Pharmacology. Drug treatments</subject><subject>Purification</subject><subject>α-Amylase</subject><issn>1570-0232</issn><issn>1873-376X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMuKFDEUhoMozkUfQcnG2VWZVCqV1EqaYUYHGkd0BHchdXLipKlLm1SL7UMN-Ao-gM9kxi6YpYuQ8Oc7Fz5CXnBWcsab15tyA7dxGrqyYqwpmS4Z54_IMddKFEI1Xx7nt1SsYJWojshJShvGuGJKPCVHvGllK6U4Jv2HXQw-gJ3DNNJuT_HH1o4OHe3ysS5NcfvvK4cUbm20MGMMPw_85HNO__wq7LDvbcJEL68_Xq1Xny7o-5s1_X1HfV6Rrko6hq8Yn5En3vYJny_3Kfl8eXFz_q5YX7-9Ol-tCxCtmAvBvG4cSAFVp7SvmLNaoZBWgnK6qTtpWwBt0bWgNGDHfSNqVdWCSai5E6fk7NB3G6dvO0yzGUIC7Hs74rRLptGtFEzwDMoDCHFKKaI32xgGG_eGM3Ov2WzMotncazZMm6w5171cBuy6Ad1D1eI1A68WwCawvY92hJAeOF3rltU6c28OHGYd3wNGkyDgCOhCRJiNm8J_VvkLCtufUA</recordid><startdate>20070201</startdate><enddate>20070201</enddate><creator>Toledo, A.L.</creator><creator>Severo, J.B.</creator><creator>Souza, R.R.</creator><creator>Campos, E.S.</creator><creator>Santana, J.C.C.</creator><creator>Tambourgi, E.B.</creator><general>Elsevier B.V</general><general>Elsevier Science</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>20070201</creationdate><title>Purification by expanded bed adsorption and characterization of an α-amylases FORILASE NTL ® from A. niger</title><author>Toledo, A.L. ; Severo, J.B. ; Souza, R.R. ; Campos, E.S. ; Santana, J.C.C. ; Tambourgi, E.B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-30f86dc53c2b78f20da87e35a5c7d864b5a9cc8aed9c78ceb1f634724305c41d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adsorption</topic><topic>alpha-Amylases - chemistry</topic><topic>alpha-Amylases - metabolism</topic><topic>Analysis</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Aspergillus niger</topic><topic>Aspergillus niger - enzymology</topic><topic>Biochemistry characterization</topic><topic>Biological and medical sciences</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Expanded bed adsorption</topic><topic>Expansion degree</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General pharmacology</topic><topic>Hydrolysis</topic><topic>Medical sciences</topic><topic>Molecular Weight</topic><topic>Pharmacology. Drug treatments</topic><topic>Purification</topic><topic>α-Amylase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Toledo, A.L.</creatorcontrib><creatorcontrib>Severo, J.B.</creatorcontrib><creatorcontrib>Souza, R.R.</creatorcontrib><creatorcontrib>Campos, E.S.</creatorcontrib><creatorcontrib>Santana, J.C.C.</creatorcontrib><creatorcontrib>Tambourgi, E.B.</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>Journal of chromatography. B, Analytical technologies in the biomedical and life sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Toledo, A.L.</au><au>Severo, J.B.</au><au>Souza, R.R.</au><au>Campos, E.S.</au><au>Santana, J.C.C.</au><au>Tambourgi, E.B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification by expanded bed adsorption and characterization of an α-amylases FORILASE NTL ® from A. niger</atitle><jtitle>Journal of chromatography. B, Analytical technologies in the biomedical and life sciences</jtitle><addtitle>J Chromatogr B Analyt Technol Biomed Life Sci</addtitle><date>2007-02-01</date><risdate>2007</risdate><volume>846</volume><issue>1</issue><spage>51</spage><epage>56</epage><pages>51-56</pages><issn>1570-0232</issn><eissn>1873-376X</eissn><abstract>In this work the purification and biochemistry characterization of α-amylases from
Aspergillus niger (FORILASE NTL
®) were studied. The effects of expansion degree of resin bed on enzyme purification by expanded bed adsorption (EBA) have also been studied. Residence time distributions (RTD) studies were done to achieve the optimal conditions of the amylases recovery on ion-exchange resin, and glucose solution was used as a new tracer. Results showed that height equivalent of the theoretical plates (HETP), axial dispersion and the Prandt number increased with bed height, bed voidage and linear velocity. The adsorption capacity of α-amylases, on the resin, increased with bed height and the best condition was at four-expansion degree. α-Amylase characterization showed that this enzyme has high affinity with soluble starch, good hydrolysis potential and molecular weight of 116
kDa.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>16959553</pmid><doi>10.1016/j.jchromb.2006.08.011</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1570-0232 |
| ispartof | Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 2007-02, Vol.846 (1), p.51-56 |
| issn | 1570-0232 1873-376X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_68953031 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Adsorption alpha-Amylases - chemistry alpha-Amylases - metabolism Analysis Analytical, structural and metabolic biochemistry Aspergillus niger Aspergillus niger - enzymology Biochemistry characterization Biological and medical sciences Electrophoresis, Polyacrylamide Gel Expanded bed adsorption Expansion degree Fundamental and applied biological sciences. Psychology General pharmacology Hydrolysis Medical sciences Molecular Weight Pharmacology. Drug treatments Purification α-Amylase |
| title | Purification by expanded bed adsorption and characterization of an α-amylases FORILASE NTL ® from A. niger |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-14T02%3A31%3A05IST&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%20by%20expanded%20bed%20adsorption%20and%20characterization%20of%20an%20%CE%B1-amylases%20FORILASE%20NTL%20%C2%AE%20from%20A.%20niger&rft.jtitle=Journal%20of%20chromatography.%20B,%20Analytical%20technologies%20in%20the%20biomedical%20and%20life%20sciences&rft.au=Toledo,%20A.L.&rft.date=2007-02-01&rft.volume=846&rft.issue=1&rft.spage=51&rft.epage=56&rft.pages=51-56&rft.issn=1570-0232&rft.eissn=1873-376X&rft_id=info:doi/10.1016/j.jchromb.2006.08.011&rft_dat=%3Cproquest_cross%3E68953031%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=68953031&rft_id=info:pmid/16959553&rft_els_id=S1570023206006647&rfr_iscdi=true |