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.

The optimal activity of a Candida rugosa lipase (Lipase OF) for hydrolysis of 2-chloroethyl ester of Ketoprofen [2-(3-benzoyphenyl) propionic acid] was at pH 4.0, while the best enantioselectivity (E) was at pH 2.2 where the enzyme was still 60% active and stable.

Lipase production and cell growth of Serratia marcescens ECU1010 were optimized in shake flasks, with lipase production being enhanced 9.5-fold (4,780 U/l) compared with the initial activity (500 U/l). Optimal carbon and nitrogen sources were Tween-80 and peptone, and the optimal ratio of Tween-80 to peptone was 1:3. The optimized cultivation conditions were 25[1]C and pH 6.5. Lipase activity, particularly specific activity, could be improved by decreasing the cultivation temperature from 35 to 25[1]C. Enzyme stability was significantly improved by simple immobilization with synthetic adsorption resin no. 8244. After five reaction cycles, enzyme activity decreased only very slightly, while enantioselectivity of the preparation remained constant, and the ees (enantiomeric excess of the remaining substrate) achieved in all cases was higher than 97%. The resin-8244-lipase preparation can be used for efficient enantioselective hydrolysis of trans-3-(4

The fermentation of an epoxide hydrolase by a newly isolated Trichosporon loubierii strain ECU1040 was optimized. The epoxide hydrolase production was enhanced by 6.9-fold from an initial activity of 45 U/l with the incorporation of substrate induction, optimization of medium composition and other culture conditions, and the implementation of a fed-batch process. It was found that phenyl glycidyl ether (PGE) could efficiently induce biosynthesis of the epoxide hydrolase, though it strongly inhibited the cell growth. To reduce the toxicity of PGE, dibutyl o-phthalate was used in flask cultivation to dissolve PGE, keeping a low concentration of PGE in the broth. Glucose was added to promote cell growth in the presence of PGE, though glycerol was identified as the best single carbon source for the highest specific activity. Trace elements have significant effect on the epoxide hydrolase synthesis.With addition of trace elements and glucose and adjustment of phosphate concentration, the total activity was enhanced by 150%. To further increase the epoxide hydrolase production, a fed-batch culture with PGE in the feed solution was performed in a 5-l jar fermenter. The maximum production of the epoxide hydrolase was 312 U/l, with a specific activity of 23.7 U/g DCW (dry cell weight).

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.