Lipase from Carica papaya latex presents high enantioselectivity toward the resolution of prodrug (R,S)-2-bromophenylacetic acid octyl ester

TETRAHEDRON LETTERS

卷:54

Article

Rivera, Ivanna^1,2,3,4  Carlos Mateos, Juan⁴  Marty, Alain^1,2,3  Sandoval, Georgina⁴  Duquesne, Sophie^1,2,3 

[1] Univ Toulouse, INP, LISBP, INSA,UPS, F-31077 Toulouse, France

[2] INRA, Ingn Syst Biol & Procedes UMR792, F-31400 Toulouse, France

[3] CNRS, UMR5504, F-31400 Toulouse, France

[4] CIATEJ, Guadalajara 44270, Jalisco, Mexico

关键词: Lipase;    Carica papaya latex;    Enantioselectivity;    2-Halogenocarboxylic acid;   

DOI  :  10.1016/j.tetlet.2013.07.151

来源: Elsevier

【 摘 要 】

Besides the well-known papain, lipolytic activity is another interesting enzymatic activity present in latex from Carica papaya. This lipolytic activity is strongly attached to the latex solid phase, resulting in a naturally immobilized biocatalyst. In this work we describe the kinetic resolution of (R,S)-2-bromophenylacetic acid octyl ester by Carica papaya crude latex and two partially purified latex fractions. Several parameters, such as substrate concentration and solvent effects were studied. The best results were obtained using decane as solvent with 50 mM of substrate and 50 mg/mL enzyme/reaction medium; under these conditions, a high enantioselectivity (E >200) was obtained with crude latex. A twofold increase of the initial rate maintaining E >200 was obtained using purified fractions without protease and without esterase. Lipase from Carica papaya latex is the most enantioselective wild-type enzyme ever described for the studied reaction. (C) 2013 Elsevier Ltd. All rights reserved.

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