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Food supplementation meets nutritional deficiencies and collagen can be used as a protein replacement food source. In general, the availability of these products consists of high molecular weight polypeptides (>300 KDa), with low body uptake, poor solubility and unpleasant taste. The application of specific enzymes makes it possible to obtain peptide fractions smaller than 30 KDa, which results in higher absorption capacity by the human body and high solubility. Bovine leather was used to obtain collagen isolate due to its high protein concentration, as it is a product of high availability and low cost and to be a potentially pollutant. The aim of this work was to evaluate 6 different enzymes (alkalase, neutrase, papain, trypsin, collagenase, and pepsin) to hydrolyze collagen isolate and identify those capable of obtaining low molecular weight peptide fractions for commercial application. For hydrolysis, 0.5 to 1.0g of enzymes/100g of collagen isolate were used, added with ultrapure water, digested for 1, 2 or 4h, under agitation, with temperature and pH adjusted according to the optimal conditions of each enzyme activity. SDS-PAGE electrophoresis was performed to estimate the molecular weight of the hydrolyzed fractions. Proximate composition analysis and solubility index were also performed. The smallest peptide fractions (<25 KDa) were obtained for papain and alkalase, all others did not show satisfactory molecular weight results. Alkalase proved to be the best option due to the lower amount of enzyme used at the same time of hydrolysis compared to papain. The hydrolyzed with alkalase, subsequently spray-dried, showed 99.2% peptides from hydrolyzed collagen isolate, 0.5% fat and 0.2% ash. Furthermore, the collagen hydrolyzed product containing peptide fractions below 25 kDa showed high solubility in cold water and no unpleasant taste perception. The product developed can be incorporated into beverages, fruit juices or beverages formulated for specific purposes.
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