Obtainment and physical-chemical and functional characterization of a lupin (Lupinus mutabilis Sweet) protein hydrolyzate

Abstract

The enzymatic or chemical modifications have been used to improve the functional properties of proteins. The first ones, generally involve the use of proteolytic enzymes to hydrolyze specific peptide bonds and its use presents certain advantages relative to the chemical methods, among them it is mentioned: its specificity, effectiveness to low concentrations and in moderate conditions and its general security make unnecessary to remove them from the final product (Ludwig et al.. 1995) The enzymatic hydrolysis originates smaller peptides and with less secondary structure, which contributes to improve certain functional properties as the solubility in a wide pH range, significant characteristic for fortification of acid drinks with protein (Jones & Tung, 1983). The use of enzymes to modify the functional properties is promising the food industry. Hydrolyzed proteins have a wide application, in the elaboration of chopped and ground meats, mix for pastries, creams for coffee, milk, mayonnaise, seasonings for salad, frozen desserts and in the pharmaceutical field, for formulation of special diets for people with allergies to proteins or who are unable to digest and absorb them.