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Study of l-aminoacylase deactivation in an ultrafiltration membrane reactor
The behaviour of an ultrafiltration membrane reactor (UFMR) (60 cm 3 of reactor volume) for the optical resolution of dl-butyrine catalysed by l-aminoacylase was studied, and the influence of substrate concentration (15–25 mmol dm −3 in N-acetyl- l-butyrine), temperature (30–50 °C) and the presence...
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Published in: | Enzyme and microbial technology 2004-08, Vol.35 (2), p.261-266 |
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container_issue | 2 |
container_start_page | 261 |
container_title | Enzyme and microbial technology |
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creator | Bódalo, Antonio Gómez, José L Gómez, Elisa Máximo, M.Fuensanta Montiel, M.Claudia |
description | The behaviour of an ultrafiltration membrane reactor (UFMR) (60
cm
3 of reactor volume) for the optical resolution of
dl-butyrine catalysed by
l-aminoacylase was studied, and the influence of substrate concentration (15–25
mmol
dm
−3 in
N-acetyl-
l-butyrine), temperature (30–50
°C) and the presence of CoCl
2 (0.5
mmol
dm
−3) on enzyme deactivation was analysed. Adsorption studies with polysulphone and regenerated cellulose membranes (30
cm
2 of filtration surface), as well as deactivation studies in the reaction conditions, were carried out to determine the causes of deactivation. A single-step deactivation scheme is proposed, and it was shown that this first-order model adequately describes enzyme deactivation. The dependence of
K
d on the enzyme concentration points to the enzyme deactivation, which is mainly caused by the adsorption phenomena on the membrane surface. |
doi_str_mv | 10.1016/j.enzmictec.2004.05.003 |
format | article |
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cm
3 of reactor volume) for the optical resolution of
dl-butyrine catalysed by
l-aminoacylase was studied, and the influence of substrate concentration (15–25
mmol
dm
−3 in
N-acetyl-
l-butyrine), temperature (30–50
°C) and the presence of CoCl
2 (0.5
mmol
dm
−3) on enzyme deactivation was analysed. Adsorption studies with polysulphone and regenerated cellulose membranes (30
cm
2 of filtration surface), as well as deactivation studies in the reaction conditions, were carried out to determine the causes of deactivation. A single-step deactivation scheme is proposed, and it was shown that this first-order model adequately describes enzyme deactivation. The dependence of
K
d on the enzyme concentration points to the enzyme deactivation, which is mainly caused by the adsorption phenomena on the membrane surface.</description><identifier>ISSN: 0141-0229</identifier><identifier>EISSN: 1879-0909</identifier><identifier>DOI: 10.1016/j.enzmictec.2004.05.003</identifier><identifier>CODEN: EMTED2</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>Bioconversions. Hemisynthesis ; Biological and medical sciences ; Biotechnology ; dl-Butyrine resolution ; Fundamental and applied biological sciences. Psychology ; l-Aminoacylase deactivation ; Methods. Procedures. Technologies ; N-Acetyl- dl-butyrine ; Ultrafiltration membrane reactor</subject><ispartof>Enzyme and microbial technology, 2004-08, Vol.35 (2), p.261-266</ispartof><rights>2004 Elsevier Inc.</rights><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c374t-fc4d3371afdf0c145c39f16fa101acca667965119ac96540a9397f10f907da4c3</citedby><cites>FETCH-LOGICAL-c374t-fc4d3371afdf0c145c39f16fa101acca667965119ac96540a9397f10f907da4c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15972653$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Bódalo, Antonio</creatorcontrib><creatorcontrib>Gómez, José L</creatorcontrib><creatorcontrib>Gómez, Elisa</creatorcontrib><creatorcontrib>Máximo, M.Fuensanta</creatorcontrib><creatorcontrib>Montiel, M.Claudia</creatorcontrib><title>Study of l-aminoacylase deactivation in an ultrafiltration membrane reactor</title><title>Enzyme and microbial technology</title><description>The behaviour of an ultrafiltration membrane reactor (UFMR) (60
cm
3 of reactor volume) for the optical resolution of
dl-butyrine catalysed by
l-aminoacylase was studied, and the influence of substrate concentration (15–25
mmol
dm
−3 in
N-acetyl-
l-butyrine), temperature (30–50
°C) and the presence of CoCl
2 (0.5
mmol
dm
−3) on enzyme deactivation was analysed. Adsorption studies with polysulphone and regenerated cellulose membranes (30
cm
2 of filtration surface), as well as deactivation studies in the reaction conditions, were carried out to determine the causes of deactivation. A single-step deactivation scheme is proposed, and it was shown that this first-order model adequately describes enzyme deactivation. The dependence of
K
d on the enzyme concentration points to the enzyme deactivation, which is mainly caused by the adsorption phenomena on the membrane surface.</description><subject>Bioconversions. Hemisynthesis</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>dl-Butyrine resolution</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>l-Aminoacylase deactivation</subject><subject>Methods. Procedures. Technologies</subject><subject>N-Acetyl- dl-butyrine</subject><subject>Ultrafiltration membrane reactor</subject><issn>0141-0229</issn><issn>1879-0909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNqFkMtOwzAQRS0EEqXwDWQDu4Rx4sR4WVW8RCUWwNoaJrbkKo9iJ5XK1-PQCpZs5kqjM497GbvkkHHg1c06M91X62gwlOUAIoMyAyiO2IzfSpWCAnXMZsAFTyHP1Sk7C2ENEBsCZuz5dRjrXdLbpEmxdV2PtGswmKQ2SIPb4uD6LnFdgl0yNoNH66b6021N--GxM4mf2N6fsxOLTTAXB52z9_u7t-Vjunp5eFouVikVUgypJVEXheRoawvERUmFsryyGO0gEVaVVFXJuUKKKgBVoaTlYBXIGgUVc3a937vx_edowqBbF8g0TfylH4PmUpa8LEQE5R4k34fgjdUb71r0O81BT-Hptf4NT0_haSh1DC9OXh1OYCBsbLRJLvyNl0rmVTlxiz1not-tM14HcqYjUztvaNB17_699Q1Kjopq</recordid><startdate>20040805</startdate><enddate>20040805</enddate><creator>Bódalo, Antonio</creator><creator>Gómez, José L</creator><creator>Gómez, Elisa</creator><creator>Máximo, M.Fuensanta</creator><creator>Montiel, M.Claudia</creator><general>Elsevier Inc</general><general>Elsevier Science</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20040805</creationdate><title>Study of l-aminoacylase deactivation in an ultrafiltration membrane reactor</title><author>Bódalo, Antonio ; Gómez, José L ; Gómez, Elisa ; Máximo, M.Fuensanta ; Montiel, M.Claudia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c374t-fc4d3371afdf0c145c39f16fa101acca667965119ac96540a9397f10f907da4c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Bioconversions. Hemisynthesis</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>dl-Butyrine resolution</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>l-Aminoacylase deactivation</topic><topic>Methods. Procedures. Technologies</topic><topic>N-Acetyl- dl-butyrine</topic><topic>Ultrafiltration membrane reactor</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bódalo, Antonio</creatorcontrib><creatorcontrib>Gómez, José L</creatorcontrib><creatorcontrib>Gómez, Elisa</creatorcontrib><creatorcontrib>Máximo, M.Fuensanta</creatorcontrib><creatorcontrib>Montiel, M.Claudia</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Enzyme and microbial technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bódalo, Antonio</au><au>Gómez, José L</au><au>Gómez, Elisa</au><au>Máximo, M.Fuensanta</au><au>Montiel, M.Claudia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Study of l-aminoacylase deactivation in an ultrafiltration membrane reactor</atitle><jtitle>Enzyme and microbial technology</jtitle><date>2004-08-05</date><risdate>2004</risdate><volume>35</volume><issue>2</issue><spage>261</spage><epage>266</epage><pages>261-266</pages><issn>0141-0229</issn><eissn>1879-0909</eissn><coden>EMTED2</coden><abstract>The behaviour of an ultrafiltration membrane reactor (UFMR) (60
cm
3 of reactor volume) for the optical resolution of
dl-butyrine catalysed by
l-aminoacylase was studied, and the influence of substrate concentration (15–25
mmol
dm
−3 in
N-acetyl-
l-butyrine), temperature (30–50
°C) and the presence of CoCl
2 (0.5
mmol
dm
−3) on enzyme deactivation was analysed. Adsorption studies with polysulphone and regenerated cellulose membranes (30
cm
2 of filtration surface), as well as deactivation studies in the reaction conditions, were carried out to determine the causes of deactivation. A single-step deactivation scheme is proposed, and it was shown that this first-order model adequately describes enzyme deactivation. The dependence of
K
d on the enzyme concentration points to the enzyme deactivation, which is mainly caused by the adsorption phenomena on the membrane surface.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><doi>10.1016/j.enzmictec.2004.05.003</doi><tpages>6</tpages></addata></record> |
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language | eng |
recordid | cdi_proquest_miscellaneous_17751534 |
source | ScienceDirect Journals |
subjects | Bioconversions. Hemisynthesis Biological and medical sciences Biotechnology dl-Butyrine resolution Fundamental and applied biological sciences. Psychology l-Aminoacylase deactivation Methods. Procedures. Technologies N-Acetyl- dl-butyrine Ultrafiltration membrane reactor |
title | Study of l-aminoacylase deactivation in an ultrafiltration membrane reactor |
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