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Información tecnológica

versión On-line ISSN 0718-0764

Resumen

ROCHA, Gabriela F; FERNANDEZ, Graciela  y  PARISI, Mónica G. Kinetic and Physicochemical Studies of an Aspartic Proteinase Isolated from Salpichroa origanifolia Fruits. Inf. tecnol. [online]. 2010, vol.21, n.2, pp.21-28. ISSN 0718-0764.  http://dx.doi.org/10.4067/S0718-07642010000200004.

A new proteolytic enzyme with milk-clotting activity was isolated from ripe fruits of Salpichroa origanifolia. Crude extract was obtained by dissolving the ethanolic powder of the fruits in 50 mM phosphate buffer pH 7.0. The enzyme presented proteolytic activity toward denatured protein substrates. Hemoglobin and casein hydrolysis were optimal in the pH range 3.5 to 6.5 at temperatures between 40 and 45°C. In addition, the crude extract showed high stability at moderate temperatures (40°C) and the proteinase activity was activated by cations such as calcium and magnesium. Degradation pattern of the bovine casein brought about by the crude extract of Salpichroa origanifolia produced higher hydrolysis degree than the commercial rennet. According to these results, it is concluded that the aspartic proteinase isolated from ripe fruits of Salpichroa origanifolia presents appropriate milk-clotting activity and thermostability properties for its use in biotechnological processes.

Palabras clave : aspartic proteinase; milk-clotting activity; kinetic characterization; proteolytic enzyme; Salpichroa origanifolia.

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