PHYSICOCHEMICAL PROPERTIES AND YIELDS OF SUNFLOWER PROTEIN ENZYMATIC HYDROLYSATES AS AFFECTED BY ENZYME AND DEFATTED SUNFLOWER MEAL

The effect of sunflower meals [industrial defatted sunflower meal (IDS M) and laboratory defatted sunflower meals (LDSM)] and enzymes (fungal protease, trypsin, and papain) on the yield and physicochemical prope rties of sunflower protein hydrolysates was investigated. The hydrolys ate was prepared from the soluble portion of a sunflower meal-enzyme s lurry after hydrolysis. Enzymatic hydrolysis solubilized a substantial portion of total protein content in all defatted sunflower meals, lea ding to a great increase in protein content of the hydrolysate. The ty pe of enzyme significantly (p <0.05) affected the product yield and pr otein recovery from IDSM. Papain gave the lowest product yield (47.4%) and protein recovery (83.8%) from IDSM substrate. More proteins were recovered from IDSM than LDSM with fungal protease. Higher protein rec overy (96.4%) and protein content (80.4%) were obtained from 1% fat LD SM hydrolyzed with papain than from 18% fat LDSM or 1% fat IDSM. Funga l protease hydrolysates possessed significant antioxidant activity. Al l hydrolysates with papain had the highest emulsion capacity. Hydrolys ate produced from a pilot-plant scale had similar characteristics to t hat from the laboratory scale. These results suggest that a proper enz yme and defatted sunflower meal should be considered for the commercia l production of the protein hydrolysates because different enzymes and meals can result in different yields, functional properties, and comp ositions of the hydrolysates.