PROFILES OF ENZYMATIC HYDROLYSIS OF DIFFERENT COLLAGENS AND DERIVATIVES OVER TIME

The interest in collagen use in the food industry to replace synthetic agents is growing every day. Among the derivatives, has the hydrolysate, which dissolves easily in water and brine, and can be incorporated into foods or drinks. The objective of this study was to determine the degree of hydrolysis (DH) of crude collagen fiber, powdered collagen fiber, gelatin and two samples of hydrolyzed collagen. The substrates were subjected to individual action of three proteolytic enzymes: papain, bromelain and collagenase (microbial origin). The substrates were incubated in sodium phosphate buffer (0.1 M, pH 7.0) on an orbital shaker at 55°C for different periods of time. In 120 minutes of hydrolysis, the crude collagen fiber showed 37.2% of DH using collagenase, the highest value compared to other substrates. The lowest values for DH were obtained for the hydrolysates collagen, with less than 1% of DH. For hydrolysis in 60 minutes, the DH values were similar to those obtained in 120 minutes of hydrolysis, with minor variations over time. The hydrolytic ability of the collagenase and bromelain was similar and superior compared with the papain.