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Biocatalytic properties of lipase in crude latex from babaco fruit (Carica pentagona)

Dhuique-Mayer C., Caro Y., Pina M., Ruales J., Dornier M., Graille J.. 2001. Biotechnology Letters, 23 (13) : p. 1021-1024.

DOI: 10.1023/A:1010552605097

Biocatalytic activities in proteolysis, lipolysis and interesterification reactions were studied for crude latex from the subtropical plant Carica pentagona. The results reveal that crude Carica pentagona latex exhibits equivalent proteolytic activities (5.73 units mg-1) and lipolytic activities (1.01 units mg-1) compared to the well-known Carica papaya, the commercially source for papain (4.57 units mg-1 and 0.90 units mg-1 respectively). Therefore, in interesterification reactions, Carica pentagona latex shows interesting lipase properties (0.77 units mg-1) higher than commercial Carica papaya latex (0.28 units mg-1).

Mots-clés : carica papaya; carica pentagona; estérase; latex; activité catalytique; lipolyse; protéolyse; triacylglycérol lipase; estérification; papaine; babaco

Article (a-revue à facteur d'impact)

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