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Original Articles

Study of Some Functional Properties of Casein: Effect of pH and Tryptic Hydrolysis

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Pages 173-183 | Received 27 Mar 2006, Accepted 10 May 2006, Published online: 31 Jan 2007

Figures & data

Figure 1 Emulsifying capacity (EC) in function of protein concentration. Each value represents the mean of triple determination. ± Standard error (vertical bars).

Figure 1 Emulsifying capacity (EC) in function of protein concentration. Each value represents the mean of triple determination. ± Standard error (vertical bars).

Figure 2 Effect of the pH and time of tryptic hydrolysis on the solubility of casein. Each value represents the mean of triple determination. ± Standard error (vertical bars).

Figure 2 Effect of the pH and time of tryptic hydrolysis on the solubility of casein. Each value represents the mean of triple determination. ± Standard error (vertical bars).

Figure 3 Effect of the pH and time of tryptic hydrolysis on the emulsifying capacity of casein. Each value represents the mean of triple determination. ± Standard error (vertical bars).

Figure 3 Effect of the pH and time of tryptic hydrolysis on the emulsifying capacity of casein. Each value represents the mean of triple determination. ± Standard error (vertical bars).

Figure 4 Effect of the pH and time of tryptic hydrolysis on the emulsifying activity index of casein. Each value represents the mean of triple determination. ± Standard error (vertical bars).

Figure 4 Effect of the pH and time of tryptic hydrolysis on the emulsifying activity index of casein. Each value represents the mean of triple determination. ± Standard error (vertical bars).

Figure 5 Effect of the pH and time of tryptic hydrolysis on the stability of the emulsion of casein. Each value represents the mean of triple determination. ± Standard error (vertical bars).

Figure 5 Effect of the pH and time of tryptic hydrolysis on the stability of the emulsion of casein. Each value represents the mean of triple determination. ± Standard error (vertical bars).

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