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The enzymatic hydrolysis through animal or vegetable proteases applied to bovine slaughtering by products makes it possible to obtain collagen originated peptides, aggregating value to these residues (Gómez-Guillén et al., 2011; Khan et al., 2011; Di Bernardini et al., 2011; Selvakumar et al., 2012; Zhang et al., 2013). The enzyme Flavourzyme has been widely used to obtain protein hydrolysates with functional properties (Kristinsson & Rasco, 2000; Yust et al., 2013; Castro & Sato, 2015; Ambigaipalan et al., 2015). Ot can act under neutral or slightly acid conditions of hydrolysis, and it is a complex fungal protease which originates from the submerged fermentation of a specific Aspergillus oryzae strain without genetic modification (Slizyte et al., 2005; Yust et al., 2013). Ultrasound has been used to change the structure and functional properties of food proteins (Chandrapala et al., 2011; Arzeni et al., 2012a), mainly proteins of animal origin (D’Sullivan et al., 2015). The use of ultrasound as a previous treatment or simultaneous to the hydrolysis process provokes the rupture of the proteins’ tertiary and quaternary structures; this is provoked by the effects of cavitation in the medium, consequently these structural changes make it easier for the enzyme to access the protein structure, provoking increase in the hydrolysis and the bioactivity (Dzuna et al., 2015). The objective of this study was to evaluate the effect of ultrasound assisted enzymatic hydrolysis (Flavourzyme) on the functional and structural properties of different bovine collagen hydrolysates. 2 Materials and methods

food science and technology

Effects of enzymatic hydrolysis (Flavourzyme®) assisted by ultrasound in the structural and functional properties of hydrolyzates from different bovine collagens