A yeast strain CGMCC 0574, identified as Trichosporon brassicae, was selected from 92 strains for its high (S) selectivity in the hydrolysis of ketoprofen ethyl ester. The effective strains of the microorganisms were isolated from soil samples with the ester as the sole carbon source. The ethyl ester proved to be the best substrate for resolution of ketoprofen among several ketoprofen esters examined. The resting cells of CGMCC 0574 could catalyze the hydrolysis of ketoprofen ethyl ester with an enantiomeric ratio of 44.9, giving (S)-ketoprofen an enantiomeric excess of 91.5% at 42% conversion. Une souche de levure désignée CGMCC 0574, identifiée comme étant Trichosporon brassicae, a été sélectionnée parmi 92 souches sur la base de sa (S)-sélectivité élevée lors de l'hydrolyse de l’ester éthylique de ketoprofen. La sélection s'est effectuée sur des souches de micro-organismes ayant été isolées à partir d'échantillons de sol avec l'ester comme seule source de carbone. L'ester éthylique s'est avéré être le meilleur substrat pour la resolution du ketoprofen parmi plusieurs esters de ketoprofen analysés. Les cellules de CGMCC 0574 au repos ont pu catalyser l'hydrolyse de l'ester éthylique de ketoprofen avec un rapport énantiomérique de 44,9, produisant du (S)-ketoprofen à 91,5% excès énantiomérique, à un taux de conversion de 42%.

Enantioselective synthesis of (S)-a-cyano-3-phenoxybenzyl alcohol [(S)-CPBA] was successfully achieved by lipase-catalyzed alcoholysis of (R,S)-CPBA acetate [(R,S)-CPBAc] in organic medium after systematic optimization of catalysts, water activity, organic solvents and acyl acceptors. A commercially available Pseudomonas fluorescens lipase, Lipase AK (Amano), showed excellent enantioselectivity (eep>99%, E=568) and high alcoholysis activity (1.88 [1]mol min−1 mg enzyme−1) towards the (S)-ester. The lipase exhibited higher activities in organic solvents with higher hydrophobicity and lower water activity controlled by anhydrous sodium sulfate. The initial rate of alcoholysis was nearly the same for alcohols of short chains (C2-C5) and the optimal concentration for n-butanol was 200-500mM. A celite-adsorbed preparation of Lipase AK was used repeatedly for eight times, without significant loss of enzyme activity.

A facile method for enzymatic glycosylation of 4-substituted benzyl alcohols and tyrosol with glucose in a monophasic aqueous-dioxane medium was reported, using a crude meal of apple seed as a new catalyst. The corresponding b-D-glucosides were synthesized in moderate yields (13.1-23.1%), among which the salidroside was obtained in 15.8% yield.

An additive method has been developed to obtain nearly optically pure (S)-ketoprofen wS.-2-(3-benzoyphenyl)propionicacid, ＞96% enantiomeric excess, eex by using lipase OFfrom Candida rugosa.for the first time. The effect of surfactantsselected as additives.on the enantioselective hydrolysis of 2-chloroethyl ester of ketoprofen by the crude and the purified C. rugosa lipase (lipase OF) was investigated. Except for Tween-60, Tween-80 and nonyl phenol polyethyleneoxy etherOP-10., most of the other surfactants tested had inhibitory influence on the lipase. As for the enantioselectivity, only Tween-80 displayed a positive effect. Moreover, the concentration of Tween-80 was found to be a sensitive factor affecting the activity and the enantioselectivity, when either the crude or the purified enzyme was used. Upon addition of the two emulsifiers at their optimal concentrations, i.e., 2%(w/v) Tween-80 and 3%(w/v) OP-10, the crude enzyme activity was greatly enhanced up to 13 and 15 times, respectively. On the other hand, the enantiomeric ratio (E value) increased from 1.2 to 6.7 for the crude lipase and from 8 to＞100 for the purified lipase in the presence of 8% or 2%(w/v) Tween-80.

A racemic glycidyl butyrate resolving strain, preliminarily identified as a Rhizopus sp., had been isolated from soil. Its extracellular lipase was found to enantioselectively hydrolyze the (S)-enantiomer of the chiral ester, with optimal activities at pH 5.3 and 42℃. Higher enantioselectivity of the enzyme was observed at lower temperatures, while the best enantioselectivity was obtained at pH 5.5-6.0, with an E value (enantiomeric ratio) of 57.