4.7 Review

Carica papaya lipase (CPL): An emerging and versatile biocatalyst

Journal

BIOTECHNOLOGY ADVANCES
Volume 24, Issue 5, Pages 493-499

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biotechadv.2006.04.002

Keywords

Carica papaya lipase; plant lipases; biocatalysis; sn-3 selectivity; ester synthesis; asymmetric resolution; amino acids

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In recent years, the Carica papaya lipase (CPL) is attracting more and more interest. This hydrolase, being tightly bonded to the water-insoluble fraction of crude papain, is thus considered as a naturally immobilized biocatalyst. To date, several CPL applications have already been described: (i) fats and oils modification, derived from the sn-3 selectivity of CPL as well as from its preference for short-chain fatty acids; (ii) esterification and inter-esterification reactions in organic media, accepting a wide range of acids and alcohols as substrates; (iii) more recently, the asymmetric resolution of different non-steroidal anti-inflammatory drugs (NSAIDs), 2-(chlorophenoxy)propionic acids, and non-natural amino acids. Taking into account the novelty and the current interest of the topic, this review aims to highlight the origin, features, and applications of the C. papaya lipase, with the objective to prompt research groups to further investigate the spectra of applications that this emerging and versatile CPL could have in the future. (c) 2006 Elsevier Inc. All rights reserved.

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