Table 1 : Kinetic resolution of 4-chloro-2-(1-hydroxyalkyl)pyridines using : Pseudomonas cepacia: lipase : Nature Protocols

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Kinetic resolution of 4-chloro-2-(1-hydroxyalkyl)pyridines using Pseudomonas cepacia lipase

Eduardo Busto, Vicente Gotor-Fernández & Vicente Gotor

Nature Protocols 1, 2061 - 2067 (2006) Published online: 30 November 2006

doi:10.1038/nprot.2006.335

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Table 1. Kinetic resolution of alcohols 1a–1d.

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Substrate	Time (h)	Excess (ee_P)^{^a}	Yield	Excess (ee_S)^{^a}	Yield	Conversion^{^b}	Enantioselectivity^{^c}
Alcohols were resolved at 30 °C and 250 r.p.m. with vinyl acetate (2) as the acyl donor, P. cepacia lipase as the biocatalyst and tetrahydrofuran as the solvent.
^a Enantiomeric excess of the (R)-ester product (ee_P) and the (S)-alcohol remaining substrate (ee_S), calculated by HPLC analysis.
^bConversion = ee_S / (ee_S + ee_p).
^cEnantioselectivity = ln[(1 - c) $times$ (1 + ee_P)] / ln[(1 - c) $times$ (1 - ee_P)].
1a	14.5	>99%	85%	>99%	88%	50%	>200
1b	14.5	>99%	82%	>99%	88%	50%	>200
1c	38	99%	97%	>99%	89%	50%	>200
1d	60	>99%	88%	>99%	89%	50%	>200

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