TY - JOUR
T1 - Investigation of lipases from various Carica papaya varieties for hydrolysis of olive oil and kinetic resolution of (R,S)-profen 2,2,2-trifluoroethyl thioesters
AU - Ng, I. Son
AU - Tsai, Shau Wei
N1 - Funding Information:
The financial support of NSC 93-2214-E-006-008 from National Science Council is appreciated.
PY - 2006/3
Y1 - 2006/3
N2 - With olive oil hydrolysis in aqueous solutions and hydrolytic resolution of (R,S)-profen 2,2,2-trifluoroethyl thioesters in water-saturated isooctane as the model systems, the lipolysis and enantioselective hydrolysis activities of four partially purified Carica papaya lipases of different plant variety and geography location of cultures were compared to select pCPL-Indo from Indonesia as the best lipase preparation. For lipolysis, an optimal pH of 8.5 for all lipase preparations was found. Yet, pCPL-Indo possessed the highest activity at pH ranged from 7 to 10. For the kinetic resolution, the thermodynamic analysis implied that pCPL-Indo has changed the conformation at 60°C and the enantiomer discrimination was dominated by ΔΔH. The kinetic analysis also indicated that the enantiomeric discrimination was mainly due to the difference of k2S and k2R in the acylation step. Agreements between experimental time-course conversions XS and best-fitted results were illustrated by considering effects of product inhibition and enzyme deactivation.
AB - With olive oil hydrolysis in aqueous solutions and hydrolytic resolution of (R,S)-profen 2,2,2-trifluoroethyl thioesters in water-saturated isooctane as the model systems, the lipolysis and enantioselective hydrolysis activities of four partially purified Carica papaya lipases of different plant variety and geography location of cultures were compared to select pCPL-Indo from Indonesia as the best lipase preparation. For lipolysis, an optimal pH of 8.5 for all lipase preparations was found. Yet, pCPL-Indo possessed the highest activity at pH ranged from 7 to 10. For the kinetic resolution, the thermodynamic analysis implied that pCPL-Indo has changed the conformation at 60°C and the enantiomer discrimination was dominated by ΔΔH. The kinetic analysis also indicated that the enantiomeric discrimination was mainly due to the difference of k2S and k2R in the acylation step. Agreements between experimental time-course conversions XS and best-fitted results were illustrated by considering effects of product inhibition and enzyme deactivation.
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U2 - 10.1016/j.procbio.2005.10.011
DO - 10.1016/j.procbio.2005.10.011
M3 - Article
AN - SCOPUS:32244432243
SN - 1359-5113
VL - 41
SP - 540
EP - 546
JO - Process Biochemistry
JF - Process Biochemistry
IS - 3
ER -