Kinetic and thermodynamic investigation of lipase - catalyzed hydrolysis of (R,S) - 3 - phenylbutyl azolides / Jin-Ru Chen in Industrial & engineering chemistry research, Vol. 51 N° 9 (Mars 2012)  

Public ISBD [article]  inIndustrial & engineering chemistry research > Vol. 51 N° 9 (Mars 2012) . - pp. 3580-3586 Titre : Kinetic and thermodynamic investigation of lipase - catalyzed hydrolysis of (R,S) - 3 - phenylbutyl azolides Type de document : texte imprimé Auteurs : Jin-Ru Chen, Auteur ; Chia-Ching Wu, Auteur ; Pei-Yun Wang, Auteur Année de publication : 2012 Article en page(s) : pp. 3580-3586 Note générale : Chimie industrielle Langues : Anglais (eng) Mots-clés : Hydrolysis Enzymatic catalysis Kinetics Résumé : Water-saturated cydohexane at 25 °C is selected as the best reaction condition for Novozym 435-catalyzed hydrolytic resolution of (R,S)-3-phenylbutyl 4-methylpyazolide (1). The kinetic constants and enantiomeric ratio of 36 are then estimated from the kinetic analysis and successfully employed for simulating the time-course conversions of both enantiomers. A feed-batch operation with water added during the reaction is proposed for converting the fast-reacting enantiomer of high concentrations to the product. A linear enthalpy-entropy compensation relationship of ―ΔΔS = ―38.84 + 3.29(―ΔΔH) with R2 = 0.98 for the lipase-catalyzed hydrolysis or alcoholysis of several (R,S)-azolides in anhydrous or water-saturated solvents is addressed. The resolution platform is further extended to (R,S)-3-(Boc-amino)-3-phenylpropionyl 4-methylpyrazolide (10), leading to improved enzyme activity and enantioselectivity if anhydrous methyl tert-butyl ether or isopropanyl ether is selected as the reaction medium. ISSN : 0888-5885 En ligne : http://cat.inist.fr/?aModele=afficheN&cpsidt=25595784 [article] Kinetic and thermodynamic investigation of lipase - catalyzed hydrolysis of (R,S) - 3 - phenylbutyl azolides [texte imprimé] / Jin-Ru Chen, Auteur ; Chia-Ching Wu, Auteur ; Pei-Yun Wang, Auteur . - 2012 . - pp. 3580-3586. Chimie industrielle Langues : Anglais (eng) in Industrial & engineering chemistry research > Vol. 51 N° 9 (Mars 2012) . - pp. 3580-3586 Mots-clés : Hydrolysis Enzymatic catalysis Kinetics Résumé : Water-saturated cydohexane at 25 °C is selected as the best reaction condition for Novozym 435-catalyzed hydrolytic resolution of (R,S)-3-phenylbutyl 4-methylpyazolide (1). The kinetic constants and enantiomeric ratio of 36 are then estimated from the kinetic analysis and successfully employed for simulating the time-course conversions of both enantiomers. A feed-batch operation with water added during the reaction is proposed for converting the fast-reacting enantiomer of high concentrations to the product. A linear enthalpy-entropy compensation relationship of ―ΔΔS = ―38.84 + 3.29(―ΔΔH) with R2 = 0.98 for the lipase-catalyzed hydrolysis or alcoholysis of several (R,S)-azolides in anhydrous or water-saturated solvents is addressed. The resolution platform is further extended to (R,S)-3-(Boc-amino)-3-phenylpropionyl 4-methylpyrazolide (10), leading to improved enzyme activity and enantioselectivity if anhydrous methyl tert-butyl ether or isopropanyl ether is selected as the reaction medium. ISSN : 0888-5885 En ligne : http://cat.inist.fr/?aModele=afficheN&cpsidt=25595784

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