Commenced in January 2007
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Modification of Palm Oil Structure to Cocoa Butter Equivalent by Carica papaya Lipase- Catalyzed Interesterification

Authors: P. Pinyaphong, S. Phutrakul

Abstract:

Palm oil could be converted to cocoa butter equivalent by lipase-catalyzed interesterification. The objective of this research was to investigate the structure modification of palm oil to cocoa butter equivalent using Carica papaya lipase –catalyzed interesterification. The study showed that the compositions of cocoa butter equivalent were affected by acyl donor sources, substrate ratio, initial water of enzyme, reaction time, reaction temperature and the amount of enzyme. Among three acyl donors tested (methyl stearate, ethyl stearate and stearic acid), methyl stearate appeared to be the best acyl donor for incorporation to palm oil structure. The best reaction conditions for cocoa butter equivalent production were : substrate ratio (palm oil : methyl stearate, mol/mol) at 1 : 4, water activity of enzyme at 0.11, reaction time at 4 h, reaction temperature at 45 ° C and 18% by weight of the enzyme. The chemical and physical properties of cocoa butter equivalent were 9.75 ± 0.41% free fatty acid, 44.89 ± 0.84 iodine number, 193.19 ± 0.78 sponification value and melting point at 37-39 °C.

Keywords: Carica papaya lipase, cocoa butter equivalent, interesterification, palm oil.

Digital Object Identifier (DOI): doi.org/10.5281/zenodo.1077056

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