Screening of lipases for the enantiomer resolution of R,S-2-octanol by esterification in organic medium

Summary Eleven commercially available lipase preparations of microbial and animal origin were screened for enantiomer resolution of R,S-2-octanol by esterification with dodecanoic acid in heptane. The influence of temperature, substrate/enzyme ratio and reaction time was studied. Among the lipases u...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Gerlach, Doris [verfasserIn] Missel, Cornelia Schreier, Peter

Format:	Artikel
Sprache:	Englisch

Erschienen:	1988

Schlagwörter:	Lipase Candida Heptan Aspergillus Niger Octanol

Anmerkung:	© Springer-Verlag 1988

Übergeordnetes Werk:	Enthalten in: Zeitschrift für Lebensmittel-Untersuchung und -Forschung - Springer-Verlag, 1943, 186(1988), 4 vom: Apr., Seite 315-318
Übergeordnetes Werk:	volume:186 ; year:1988 ; number:4 ; month:04 ; pages:315-318

Links:	Volltext

DOI / URN:	10.1007/BF01027034

Katalog-ID:	OLC2029935565

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520			\|a Summary Eleven commercially available lipase preparations of microbial and animal origin were screened for enantiomer resolution of R,S-2-octanol by esterification with dodecanoic acid in heptane. The influence of temperature, substrate/enzyme ratio and reaction time was studied. Among the lipases used, three microbial (2212 D, Röhm,Aspergillus niger; MY, Meito Sangyo,Candida cylindracea; S 80000, Gist-Brocades,Rhizopus arrhizus) and three porcine pancreas lipases (MKC, Sigma, Röhm) showed the highest rates of ester formation (13%–67%), in which (R)-(−)-2-octanol was predominantly selected by the enzymes. Quantitative capillary gas chromatography (HRGC) revealed “ee” values for the ester, ranging from 10% to 83%. Enantioselectivity was influenced, in part, by the temperature used. For microbial lipases, increasing the temperature led to a decrease of the enantioselectivity, whereas at 40 °C and 70 °C similar “ee” values were observed for porcine pancreas lipases.
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allfields	10.1007/BF01027034 doi (DE-627)OLC2029935565 (DE-He213)BF01027034-p DE-627 ger DE-627 rakwb eng 630 640 VZ Gerlach, Doris verfasserin aut Screening of lipases for the enantiomer resolution of R,S-2-octanol by esterification in organic medium 1988 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1988 Summary Eleven commercially available lipase preparations of microbial and animal origin were screened for enantiomer resolution of R,S-2-octanol by esterification with dodecanoic acid in heptane. The influence of temperature, substrate/enzyme ratio and reaction time was studied. Among the lipases used, three microbial (2212 D, Röhm,Aspergillus niger; MY, Meito Sangyo,Candida cylindracea; S 80000, Gist-Brocades,Rhizopus arrhizus) and three porcine pancreas lipases (MKC, Sigma, Röhm) showed the highest rates of ester formation (13%–67%), in which (R)-(−)-2-octanol was predominantly selected by the enzymes. Quantitative capillary gas chromatography (HRGC) revealed “ee” values for the ester, ranging from 10% to 83%. Enantioselectivity was influenced, in part, by the temperature used. For microbial lipases, increasing the temperature led to a decrease of the enantioselectivity, whereas at 40 °C and 70 °C similar “ee” values were observed for porcine pancreas lipases. Lipase Candida Heptan Aspergillus Niger Octanol Missel, Cornelia aut Schreier, Peter aut Enthalten in Zeitschrift für Lebensmittel-Untersuchung und -Forschung Springer-Verlag, 1943 186(1988), 4 vom: Apr., Seite 315-318 (DE-627)12947407X (DE-600)203000-7 (DE-576)01485192X 0044-3026 nnns volume:186 year:1988 number:4 month:04 pages:315-318 https://doi.org/10.1007/BF01027034 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_40 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_183 GBV_ILN_252 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2010 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4103 GBV_ILN_4193 GBV_ILN_4219 GBV_ILN_4247 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4319 GBV_ILN_4328 AR 186 1988 4 04 315-318
spelling	10.1007/BF01027034 doi (DE-627)OLC2029935565 (DE-He213)BF01027034-p DE-627 ger DE-627 rakwb eng 630 640 VZ Gerlach, Doris verfasserin aut Screening of lipases for the enantiomer resolution of R,S-2-octanol by esterification in organic medium 1988 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1988 Summary Eleven commercially available lipase preparations of microbial and animal origin were screened for enantiomer resolution of R,S-2-octanol by esterification with dodecanoic acid in heptane. The influence of temperature, substrate/enzyme ratio and reaction time was studied. Among the lipases used, three microbial (2212 D, Röhm,Aspergillus niger; MY, Meito Sangyo,Candida cylindracea; S 80000, Gist-Brocades,Rhizopus arrhizus) and three porcine pancreas lipases (MKC, Sigma, Röhm) showed the highest rates of ester formation (13%–67%), in which (R)-(−)-2-octanol was predominantly selected by the enzymes. Quantitative capillary gas chromatography (HRGC) revealed “ee” values for the ester, ranging from 10% to 83%. Enantioselectivity was influenced, in part, by the temperature used. For microbial lipases, increasing the temperature led to a decrease of the enantioselectivity, whereas at 40 °C and 70 °C similar “ee” values were observed for porcine pancreas lipases. Lipase Candida Heptan Aspergillus Niger Octanol Missel, Cornelia aut Schreier, Peter aut Enthalten in Zeitschrift für Lebensmittel-Untersuchung und -Forschung Springer-Verlag, 1943 186(1988), 4 vom: Apr., Seite 315-318 (DE-627)12947407X (DE-600)203000-7 (DE-576)01485192X 0044-3026 nnns volume:186 year:1988 number:4 month:04 pages:315-318 https://doi.org/10.1007/BF01027034 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_40 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_183 GBV_ILN_252 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2010 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4103 GBV_ILN_4193 GBV_ILN_4219 GBV_ILN_4247 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4319 GBV_ILN_4328 AR 186 1988 4 04 315-318
allfields_unstemmed	10.1007/BF01027034 doi (DE-627)OLC2029935565 (DE-He213)BF01027034-p DE-627 ger DE-627 rakwb eng 630 640 VZ Gerlach, Doris verfasserin aut Screening of lipases for the enantiomer resolution of R,S-2-octanol by esterification in organic medium 1988 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1988 Summary Eleven commercially available lipase preparations of microbial and animal origin were screened for enantiomer resolution of R,S-2-octanol by esterification with dodecanoic acid in heptane. The influence of temperature, substrate/enzyme ratio and reaction time was studied. Among the lipases used, three microbial (2212 D, Röhm,Aspergillus niger; MY, Meito Sangyo,Candida cylindracea; S 80000, Gist-Brocades,Rhizopus arrhizus) and three porcine pancreas lipases (MKC, Sigma, Röhm) showed the highest rates of ester formation (13%–67%), in which (R)-(−)-2-octanol was predominantly selected by the enzymes. Quantitative capillary gas chromatography (HRGC) revealed “ee” values for the ester, ranging from 10% to 83%. Enantioselectivity was influenced, in part, by the temperature used. For microbial lipases, increasing the temperature led to a decrease of the enantioselectivity, whereas at 40 °C and 70 °C similar “ee” values were observed for porcine pancreas lipases. Lipase Candida Heptan Aspergillus Niger Octanol Missel, Cornelia aut Schreier, Peter aut Enthalten in Zeitschrift für Lebensmittel-Untersuchung und -Forschung Springer-Verlag, 1943 186(1988), 4 vom: Apr., Seite 315-318 (DE-627)12947407X (DE-600)203000-7 (DE-576)01485192X 0044-3026 nnns volume:186 year:1988 number:4 month:04 pages:315-318 https://doi.org/10.1007/BF01027034 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_40 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_183 GBV_ILN_252 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2010 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4103 GBV_ILN_4193 GBV_ILN_4219 GBV_ILN_4247 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4319 GBV_ILN_4328 AR 186 1988 4 04 315-318
allfieldsGer	10.1007/BF01027034 doi (DE-627)OLC2029935565 (DE-He213)BF01027034-p DE-627 ger DE-627 rakwb eng 630 640 VZ Gerlach, Doris verfasserin aut Screening of lipases for the enantiomer resolution of R,S-2-octanol by esterification in organic medium 1988 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1988 Summary Eleven commercially available lipase preparations of microbial and animal origin were screened for enantiomer resolution of R,S-2-octanol by esterification with dodecanoic acid in heptane. The influence of temperature, substrate/enzyme ratio and reaction time was studied. Among the lipases used, three microbial (2212 D, Röhm,Aspergillus niger; MY, Meito Sangyo,Candida cylindracea; S 80000, Gist-Brocades,Rhizopus arrhizus) and three porcine pancreas lipases (MKC, Sigma, Röhm) showed the highest rates of ester formation (13%–67%), in which (R)-(−)-2-octanol was predominantly selected by the enzymes. Quantitative capillary gas chromatography (HRGC) revealed “ee” values for the ester, ranging from 10% to 83%. Enantioselectivity was influenced, in part, by the temperature used. For microbial lipases, increasing the temperature led to a decrease of the enantioselectivity, whereas at 40 °C and 70 °C similar “ee” values were observed for porcine pancreas lipases. Lipase Candida Heptan Aspergillus Niger Octanol Missel, Cornelia aut Schreier, Peter aut Enthalten in Zeitschrift für Lebensmittel-Untersuchung und -Forschung Springer-Verlag, 1943 186(1988), 4 vom: Apr., Seite 315-318 (DE-627)12947407X (DE-600)203000-7 (DE-576)01485192X 0044-3026 nnns volume:186 year:1988 number:4 month:04 pages:315-318 https://doi.org/10.1007/BF01027034 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_40 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_183 GBV_ILN_252 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2010 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4103 GBV_ILN_4193 GBV_ILN_4219 GBV_ILN_4247 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4319 GBV_ILN_4328 AR 186 1988 4 04 315-318
allfieldsSound	10.1007/BF01027034 doi (DE-627)OLC2029935565 (DE-He213)BF01027034-p DE-627 ger DE-627 rakwb eng 630 640 VZ Gerlach, Doris verfasserin aut Screening of lipases for the enantiomer resolution of R,S-2-octanol by esterification in organic medium 1988 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1988 Summary Eleven commercially available lipase preparations of microbial and animal origin were screened for enantiomer resolution of R,S-2-octanol by esterification with dodecanoic acid in heptane. The influence of temperature, substrate/enzyme ratio and reaction time was studied. Among the lipases used, three microbial (2212 D, Röhm,Aspergillus niger; MY, Meito Sangyo,Candida cylindracea; S 80000, Gist-Brocades,Rhizopus arrhizus) and three porcine pancreas lipases (MKC, Sigma, Röhm) showed the highest rates of ester formation (13%–67%), in which (R)-(−)-2-octanol was predominantly selected by the enzymes. Quantitative capillary gas chromatography (HRGC) revealed “ee” values for the ester, ranging from 10% to 83%. Enantioselectivity was influenced, in part, by the temperature used. For microbial lipases, increasing the temperature led to a decrease of the enantioselectivity, whereas at 40 °C and 70 °C similar “ee” values were observed for porcine pancreas lipases. Lipase Candida Heptan Aspergillus Niger Octanol Missel, Cornelia aut Schreier, Peter aut Enthalten in Zeitschrift für Lebensmittel-Untersuchung und -Forschung Springer-Verlag, 1943 186(1988), 4 vom: Apr., Seite 315-318 (DE-627)12947407X (DE-600)203000-7 (DE-576)01485192X 0044-3026 nnns volume:186 year:1988 number:4 month:04 pages:315-318 https://doi.org/10.1007/BF01027034 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_40 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_183 GBV_ILN_252 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2010 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4103 GBV_ILN_4193 GBV_ILN_4219 GBV_ILN_4247 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4319 GBV_ILN_4328 AR 186 1988 4 04 315-318
language	English
source	Enthalten in Zeitschrift für Lebensmittel-Untersuchung und -Forschung 186(1988), 4 vom: Apr., Seite 315-318 volume:186 year:1988 number:4 month:04 pages:315-318
sourceStr	Enthalten in Zeitschrift für Lebensmittel-Untersuchung und -Forschung 186(1988), 4 vom: Apr., Seite 315-318 volume:186 year:1988 number:4 month:04 pages:315-318
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Lipase Candida Heptan Aspergillus Niger Octanol
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container_title	Zeitschrift für Lebensmittel-Untersuchung und -Forschung
authorswithroles_txt_mv	Gerlach, Doris @@aut@@ Missel, Cornelia @@aut@@ Schreier, Peter @@aut@@
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author	Gerlach, Doris
spellingShingle	Gerlach, Doris ddc 630 misc Lipase misc Candida misc Heptan misc Aspergillus Niger misc Octanol Screening of lipases for the enantiomer resolution of R,S-2-octanol by esterification in organic medium
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topic_title	630 640 VZ Screening of lipases for the enantiomer resolution of R,S-2-octanol by esterification in organic medium Lipase Candida Heptan Aspergillus Niger Octanol
topic	ddc 630 misc Lipase misc Candida misc Heptan misc Aspergillus Niger misc Octanol
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title	Screening of lipases for the enantiomer resolution of R,S-2-octanol by esterification in organic medium
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title_full	Screening of lipases for the enantiomer resolution of R,S-2-octanol by esterification in organic medium
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title_sort	screening of lipases for the enantiomer resolution of r,s-2-octanol by esterification in organic medium
title_auth	Screening of lipases for the enantiomer resolution of R,S-2-octanol by esterification in organic medium
abstract	Summary Eleven commercially available lipase preparations of microbial and animal origin were screened for enantiomer resolution of R,S-2-octanol by esterification with dodecanoic acid in heptane. The influence of temperature, substrate/enzyme ratio and reaction time was studied. Among the lipases used, three microbial (2212 D, Röhm,Aspergillus niger; MY, Meito Sangyo,Candida cylindracea; S 80000, Gist-Brocades,Rhizopus arrhizus) and three porcine pancreas lipases (MKC, Sigma, Röhm) showed the highest rates of ester formation (13%–67%), in which (R)-(−)-2-octanol was predominantly selected by the enzymes. Quantitative capillary gas chromatography (HRGC) revealed “ee” values for the ester, ranging from 10% to 83%. Enantioselectivity was influenced, in part, by the temperature used. For microbial lipases, increasing the temperature led to a decrease of the enantioselectivity, whereas at 40 °C and 70 °C similar “ee” values were observed for porcine pancreas lipases. © Springer-Verlag 1988
abstractGer	Summary Eleven commercially available lipase preparations of microbial and animal origin were screened for enantiomer resolution of R,S-2-octanol by esterification with dodecanoic acid in heptane. The influence of temperature, substrate/enzyme ratio and reaction time was studied. Among the lipases used, three microbial (2212 D, Röhm,Aspergillus niger; MY, Meito Sangyo,Candida cylindracea; S 80000, Gist-Brocades,Rhizopus arrhizus) and three porcine pancreas lipases (MKC, Sigma, Röhm) showed the highest rates of ester formation (13%–67%), in which (R)-(−)-2-octanol was predominantly selected by the enzymes. Quantitative capillary gas chromatography (HRGC) revealed “ee” values for the ester, ranging from 10% to 83%. Enantioselectivity was influenced, in part, by the temperature used. For microbial lipases, increasing the temperature led to a decrease of the enantioselectivity, whereas at 40 °C and 70 °C similar “ee” values were observed for porcine pancreas lipases. © Springer-Verlag 1988
abstract_unstemmed	Summary Eleven commercially available lipase preparations of microbial and animal origin were screened for enantiomer resolution of R,S-2-octanol by esterification with dodecanoic acid in heptane. The influence of temperature, substrate/enzyme ratio and reaction time was studied. Among the lipases used, three microbial (2212 D, Röhm,Aspergillus niger; MY, Meito Sangyo,Candida cylindracea; S 80000, Gist-Brocades,Rhizopus arrhizus) and three porcine pancreas lipases (MKC, Sigma, Röhm) showed the highest rates of ester formation (13%–67%), in which (R)-(−)-2-octanol was predominantly selected by the enzymes. Quantitative capillary gas chromatography (HRGC) revealed “ee” values for the ester, ranging from 10% to 83%. Enantioselectivity was influenced, in part, by the temperature used. For microbial lipases, increasing the temperature led to a decrease of the enantioselectivity, whereas at 40 °C and 70 °C similar “ee” values were observed for porcine pancreas lipases. © Springer-Verlag 1988
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title_short	Screening of lipases for the enantiomer resolution of R,S-2-octanol by esterification in organic medium
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