Covalent immobilization of pure lipases A and B from Candida rugosa
Covalent immobilization on agarose and SiO 2 of pure lipase A (LIP.A) and B (LIP.B) from C. rugosa is described. The results obtained are compared with the data obtained in the covalent binding of commercial lipase (CL) to the same supports. The immobilization of LIP.A and LIP.B on agarose affords m...
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Veröffentlicht in: | Journal of molecular catalysis. B, Enzymatic Enzymatic, 1997-01, Vol.2 (4), p.177-184 |
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container_title | Journal of molecular catalysis. B, Enzymatic |
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creator | Moreno, JoséM Hernaiz, María J Sánchez-Montero, JoséM Sinisterra, JoséV Bustos, M.Teresa Sánchez, M.Eva Bello, JoséF |
description | Covalent immobilization on agarose and SiO
2 of pure lipase A (LIP.A) and B (LIP.B) from
C. rugosa is described. The results obtained are compared with the data obtained in the covalent binding of commercial lipase (CL) to the same supports. The immobilization of LIP.A and LIP.B on agarose affords more stable biocatalysts than on SiO
2. Kinetic studies of all these lipases and derivatives in the hydrolysis of (
R)-(+) and (
S)-(−) methyl 2-chloropropionates were performed and their enantiomeric ratios (
E =
(
V
max
K
m
)
fast
(
V
max
K
m
)
slow
) calculated. The results show that (i) purification of the commercial lipase increased the
E value 2.5-fold; (ii) both isoenzymes have similar
E values, and (iii) in general, the
E value increases with the immobilization process. |
doi_str_mv | 10.1016/S1381-1177(96)00029-X |
format | Article |
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2 of pure lipase A (LIP.A) and B (LIP.B) from
C. rugosa is described. The results obtained are compared with the data obtained in the covalent binding of commercial lipase (CL) to the same supports. The immobilization of LIP.A and LIP.B on agarose affords more stable biocatalysts than on SiO
2. Kinetic studies of all these lipases and derivatives in the hydrolysis of (
R)-(+) and (
S)-(−) methyl 2-chloropropionates were performed and their enantiomeric ratios (
E =
(
V
max
K
m
)
fast
(
V
max
K
m
)
slow
) calculated. The results show that (i) purification of the commercial lipase increased the
E value 2.5-fold; (ii) both isoenzymes have similar
E values, and (iii) in general, the
E value increases with the immobilization process.</description><identifier>ISSN: 1381-1177</identifier><identifier>EISSN: 1873-3158</identifier><identifier>DOI: 10.1016/S1381-1177(96)00029-X</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Biological and medical sciences ; Biotechnology ; Candida rugosa ; Fundamental and applied biological sciences. Psychology ; Immobilization ; Immobilization of enzymes and other molecules ; Immobilization techniques ; Lipases ; Methods. Procedures. Technologies</subject><ispartof>Journal of molecular catalysis. B, Enzymatic, 1997-01, Vol.2 (4), p.177-184</ispartof><rights>1997</rights><rights>1997 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c403t-db053f4db0999d11a8f323fec87f816c937593f8d957cc50b64a3acffb4153983</citedby><cites>FETCH-LOGICAL-c403t-db053f4db0999d11a8f323fec87f816c937593f8d957cc50b64a3acffb4153983</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S1381-1177(96)00029-X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2571484$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Moreno, JoséM</creatorcontrib><creatorcontrib>Hernaiz, María J</creatorcontrib><creatorcontrib>Sánchez-Montero, JoséM</creatorcontrib><creatorcontrib>Sinisterra, JoséV</creatorcontrib><creatorcontrib>Bustos, M.Teresa</creatorcontrib><creatorcontrib>Sánchez, M.Eva</creatorcontrib><creatorcontrib>Bello, JoséF</creatorcontrib><title>Covalent immobilization of pure lipases A and B from Candida rugosa</title><title>Journal of molecular catalysis. B, Enzymatic</title><description>Covalent immobilization on agarose and SiO
2 of pure lipase A (LIP.A) and B (LIP.B) from
C. rugosa is described. The results obtained are compared with the data obtained in the covalent binding of commercial lipase (CL) to the same supports. The immobilization of LIP.A and LIP.B on agarose affords more stable biocatalysts than on SiO
2. Kinetic studies of all these lipases and derivatives in the hydrolysis of (
R)-(+) and (
S)-(−) methyl 2-chloropropionates were performed and their enantiomeric ratios (
E =
(
V
max
K
m
)
fast
(
V
max
K
m
)
slow
) calculated. The results show that (i) purification of the commercial lipase increased the
E value 2.5-fold; (ii) both isoenzymes have similar
E values, and (iii) in general, the
E value increases with the immobilization process.</description><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Candida rugosa</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immobilization</subject><subject>Immobilization of enzymes and other molecules</subject><subject>Immobilization techniques</subject><subject>Lipases</subject><subject>Methods. Procedures. Technologies</subject><issn>1381-1177</issn><issn>1873-3158</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><recordid>eNqFkEtLxDAUhYMoOI7-BCELEV1UcydNm6xkLL5gwIUKswtpmkikbWrSDuivt_PQratzFt-5h3sQOgVyBQSy6xegHBKAPL8Q2SUhZCaS5R6aAM9pQoHx_dH_IofoKMaPNQTAJ6go_ErVpu2xaxpfutp9q975FnuLuyEYXLtORRPxHKu2wrfYBt_gYvSuUjgM7z6qY3RgVR3NyU6n6O3-7rV4TBbPD0_FfJHolNA-qUrCqE1HEUJUAIpbOqPWaJ5bDpkWNGeCWl4JlmvNSJmliiptbZkCo4LTKTrf3u2C_xxM7GXjojZ1rVrjhyghI4TnQowg24I6-BiDsbILrlHhSwKR68nkZjK53kOKTG4mk8sxd7YrUFGr2gbVahf_wjOWQ8rTEbvZYmZ8duVMkFE702pTuWB0Lyvv_in6AYnjf2M</recordid><startdate>19970101</startdate><enddate>19970101</enddate><creator>Moreno, JoséM</creator><creator>Hernaiz, María J</creator><creator>Sánchez-Montero, JoséM</creator><creator>Sinisterra, JoséV</creator><creator>Bustos, M.Teresa</creator><creator>Sánchez, M.Eva</creator><creator>Bello, JoséF</creator><general>Elsevier B.V</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>19970101</creationdate><title>Covalent immobilization of pure lipases A and B from Candida rugosa</title><author>Moreno, JoséM ; Hernaiz, María J ; Sánchez-Montero, JoséM ; Sinisterra, JoséV ; Bustos, M.Teresa ; Sánchez, M.Eva ; Bello, JoséF</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c403t-db053f4db0999d11a8f323fec87f816c937593f8d957cc50b64a3acffb4153983</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Candida rugosa</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Immobilization</topic><topic>Immobilization of enzymes and other molecules</topic><topic>Immobilization techniques</topic><topic>Lipases</topic><topic>Methods. Procedures. Technologies</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moreno, JoséM</creatorcontrib><creatorcontrib>Hernaiz, María J</creatorcontrib><creatorcontrib>Sánchez-Montero, JoséM</creatorcontrib><creatorcontrib>Sinisterra, JoséV</creatorcontrib><creatorcontrib>Bustos, M.Teresa</creatorcontrib><creatorcontrib>Sánchez, M.Eva</creatorcontrib><creatorcontrib>Bello, JoséF</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>Journal of molecular catalysis. B, Enzymatic</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moreno, JoséM</au><au>Hernaiz, María J</au><au>Sánchez-Montero, JoséM</au><au>Sinisterra, JoséV</au><au>Bustos, M.Teresa</au><au>Sánchez, M.Eva</au><au>Bello, JoséF</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Covalent immobilization of pure lipases A and B from Candida rugosa</atitle><jtitle>Journal of molecular catalysis. B, Enzymatic</jtitle><date>1997-01-01</date><risdate>1997</risdate><volume>2</volume><issue>4</issue><spage>177</spage><epage>184</epage><pages>177-184</pages><issn>1381-1177</issn><eissn>1873-3158</eissn><abstract>Covalent immobilization on agarose and SiO
2 of pure lipase A (LIP.A) and B (LIP.B) from
C. rugosa is described. The results obtained are compared with the data obtained in the covalent binding of commercial lipase (CL) to the same supports. The immobilization of LIP.A and LIP.B on agarose affords more stable biocatalysts than on SiO
2. Kinetic studies of all these lipases and derivatives in the hydrolysis of (
R)-(+) and (
S)-(−) methyl 2-chloropropionates were performed and their enantiomeric ratios (
E =
(
V
max
K
m
)
fast
(
V
max
K
m
)
slow
) calculated. The results show that (i) purification of the commercial lipase increased the
E value 2.5-fold; (ii) both isoenzymes have similar
E values, and (iii) in general, the
E value increases with the immobilization process.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><doi>10.1016/S1381-1177(96)00029-X</doi><tpages>8</tpages></addata></record> |
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ispartof | Journal of molecular catalysis. B, Enzymatic, 1997-01, Vol.2 (4), p.177-184 |
issn | 1381-1177 1873-3158 |
language | eng |
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source | Access via ScienceDirect (Elsevier) |
subjects | Biological and medical sciences Biotechnology Candida rugosa Fundamental and applied biological sciences. Psychology Immobilization Immobilization of enzymes and other molecules Immobilization techniques Lipases Methods. Procedures. Technologies |
title | Covalent immobilization of pure lipases A and B from Candida rugosa |
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