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In this work the hydrolytic activity of the extract from Salpichroa origanifolia ripe fruits on bovine, ovine and caprine caseins was studied. The enzymatic reaction was carried out at pH 6.2 and 37°C of temperature for twenty hours. Peptides obtained from the enzymatic hydrolysis of all caseins were quantified by spectrophotometry and analyzed by tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis (tricine-SDS-PAGE) and densitometry. Casein hydrolysates were separated by ultrafiltration obtaining higher and lower fractions of 3 kDa molecular mass. Statistical analysis of the caseins hydrolysis was significant for the time of hydrolysis and the type of casein (p<0.05). A higher degree of hydrolysis of caprine casein was observed after 20 hours of incubation. Antimicrobial activity of the hydrolysates was assessed and it was found that less than 3 kDa molecular mass peptides from bovine and ovine caseins showed the highest inhibitory effect on the evaluated microorganisms.

Péptidos con Actividad Antimicrobiana obtenidos de Proteínas Lácteas con Extractos de Salpichroa origanifolia