Abstract
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.
Highlights
In recent years, there is an increasing interest in the intentional modification of proteins to obtain the protein hydrolysates, these with many uses in foods for special purposes such as non-allergenic formulations of infant, geriatric food, sports drinks, and dietetic food (DAMODARAN et al, 2010)
The most widely used parameter to describe the result of a hydrolysis process is the Degree of Hydrolysis (DH) (BENITEZ et al, 2008), defined as the fraction of cleaved peptide bonds, which is usually expressed as a percentage (DAMODARAN et al, 2010)
Smaller DEGREE OF HYDROLYSIS (DH) values were obtained for the collagen hydrolysate B, with DH average values of less than 1 %, suggesting that this substrate has been almost completely hydrolyzed in the manufacturing process, different from the hydrolyzed collagen A
Summary
There is an increasing interest in the intentional modification of proteins to obtain the protein hydrolysates, these with many uses in foods for special purposes such as non-allergenic formulations of infant, geriatric food, sports drinks, and dietetic food (DAMODARAN et al, 2010). These hydrolysates can be obtained by chemical or enzymatic hydrolysis (KOBLITZ, 2008). Gelatin is obtained from collagen using acid or alkaline hydrolysis. Collagen hydrolysate is obtained by chemical or enzymatic hydrolysis under controlled conditions (SCHRIEBER; GAREIS, 2007, WANG et al, 2009)
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