PARTIAL PURIFICATION OF PROTEOLYTIC ENZYMES AND CHARACTERIZATION OF TRYPSIN FROM MERLUCCIUS HUBBSI BY-PRODUCTS

DANIELA LAMAS; MARIA ISABEL YEANNES; AGUEDA MASSA

International Journal of Food and Nutritional Sciences

IJFANS

Lugar: Nueva Delhi; Año: 2015 vol. 4 p. 121 - 130

Proteolytic enzymes have beendetected and partially purified from Merlucciushubbsi viscera. Crude proteinase extract exhibited its maximal activity at pH 7.94, 59.52ºC and 33.93 minutes using azocaseín as a substrate. The molecular weight wasestimated to be 25 kDa by SDS-PAGE. The best ratio of crude extract to coldacetone for the partial purification of protease was found in 1:1.25 with a 94.02% of recovery. Results relative to the substratespecific BAPNA, indicated that the recovered protease was a trypsin. Thekinetic trypsin constant Km and kcat were 0.38 mM and 0.97/srespectively, while the catalytic efficiency was 2.54/mMs. The stabilityresults obtained with surfactants suggest that this enzyme can be incorporatedas an ingredient in detergent formulations.