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Comparison of the lipase activity in hydrolysis and acyl transfer reactions of two latex plant extracts from babaco (Vasconcellea x Heilbornii Cv.) and Plumeria rubra : Effect of the aqueous microenvironment

Cambon E., Gouzou F., Pina M., Baréa B., Barouh N., Lago R.C.A., Ruales J., Shau-Wei Tsai, Villeneuve P.. 2006. Journal of Agricultural and Food Chemistry, 54 (7) : p. 2726-2731.

DOI: 10.1021/jf052505k

The enzymatic properties of Plumeria rubra latex have been evaluated for the first time, showing a high activity in both hydrolysis and synthesis reactions, and compared to the biocatalytic behavior of babaco (Vasconcellea x Heilbornii cv.) latex. Both biocatalysts have been optimized by studying the various parameters that influence reaction kinetics. The optimum temperatures for hydrolysis reactions were 50 and 55°C for babaco and Plumeria, respectively. The optimum pH for babaco latex was 7, whereas for Plumeria latex, two optimal pH values (4 and 7) were observed. With regard to esterification and acyl transfer reactions such as alcoholysis and interesterification, the influence of thermodynamic water activity on reaction yields was determined and correlated with water sorption and desorption isotherms. When babaco latex is used as a biocatalyst, optimal synthesis reaction yields are obtained when the enzymatic extract is stabilized at a water activity value of 0.38, which corresponds to a water content of 5.7%. This optimal level of hydration is located on the linear portion of the biocatalyst's sorption isotherm, where the water molecules exhibit high-energy interactions with the protein network. In synthesis reactions (esterification, alcoholysis, and interesterification) biocatalyzed by Plumeria latex, correlation between best reaction yields and water activity cannot be done. Indeed, the sorption isotherm plot has an atypical shape, indicating that water might be trapped in the latex matrix and, consequently, that the water content of the biocatalyst is highly dependent on the hydration history of the latex.

Mots-clés : latex; estérase; activité enzymatique; hydrolyse enzymatique; acylation; catalyseur; lipase; plumeria rubra; vasconcellea

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