Titlebook: Biocatalysis; Herfried Griengl Book 2000 Springer-Verlag Wien 2000 Biotechnology.Organische Chemie.biocatalysis.biotechnology/Biokatalyse.

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Psychotropic Drugs and the Perinatal Period form a monolayer on the resin surface, and adsorption is complete within 2 min AJ270 can be entrapped in agar and agarose gels (optimum loading: 20 mg dry weight bacteria per cm3 gel). Adsorption and entrapment improve amidase thermal stability 3-4 fold, and entrapment shifts the pH optimum from 8

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Terrace

Kylee Trevillion,Trudi Seneviratneof thioanisole. When H202 was added stepwise to MPO, a maximal yield of 78% was obtained at pH 5 (ee 23%), whereas an optimum in the enantiomeric excess (32%, (R)-sulfoxide) was found at pH 6 (60% yield). For MnP a yield of 18% and a high enantiomeric excess of 91% of the (S)-sulfoxide were obtained

Obituary

Parent-Infant Interaction Assessmentorseradish peroxidase (HRP) catalyzed kinetic resolution of the ene product. The highest enantiomeric excess (up to 95%) has been obtained for the isopropyl ester threo-4c, which establishes that the size of the remote ester functionality exercises appreciable control in the enantioselectivity of th

Grievance

Lipase-Catalyzed Synthesis of Carboxylic,rally in anhydrous organic media to avoid undesirable hydrolysis of the ester. Alternatively, carboxylic amides can be synthesized by lipase mediated condensation of carboxylic acids and amines if an excess of either reactant is avoided.

guzzle

Lipase-Catalyzed Resolution of Ibuprofen,ansesterification or hydrolysis of the ibuprofen ethyl ester (E<2, 28-48 h), the reaction with vinylesters occurred significantly faster (1.5-5 h) and with considerably higher enantioselectivity (E=8-39).

Commentary

,Synthesis of Optically Active a-Methyl ß-Hydroperoxy Esters by Diastereoselective Singlet Oxygen Enorseradish peroxidase (HRP) catalyzed kinetic resolution of the ene product. The highest enantiomeric excess (up to 95%) has been obtained for the isopropyl ester threo-4c, which establishes that the size of the remote ester functionality exercises appreciable control in the enantioselectivity of the enzymatic kinetic resolution.

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