The in vitro protein digestibility of the samples was determined
by the modified method of Hsu, Vavak, Satterlee, and Miller (1977).
Briefly, 50 ml of aqueous protein suspension containing 6.25 mg
protein/ml was prepared. Then, samples were placed in a 37 C
water bath and the pH was adjusted to 8.00 using 0.1 M NaOH
and/or 0.1 M HCl, while stirring. Trypsin at a concentration of
1.6 mg/ml was maintained in an ice bath and the pH was adjusted
to 8.00 with 0.1 M NaOH and/or 0.1 M HCl. Five millilitres of
enzyme solution were then added to the protein suspension, which
was kept stirred at 37 C. The trypsin had an activity of 13,766
BAEE units/mg protein. The pH drop was recorded at 15 s after
enzyme addition and at one minute intervals for 10 min. The
enzyme solution was always freshly prepared before each series
of experiments. The percent protein digestibility (Y) was calculated
by using Eq. (1) (Hsu et al., 1977):
Y ¼ 210:464 18:1x; ð1Þ
where x is the change in pH after 10 min.
The in vitro protein digestibility of the samples was determinedby the modified method of Hsu, Vavak, Satterlee, and Miller (1977).Briefly, 50 ml of aqueous protein suspension containing 6.25 mgprotein/ml was prepared. Then, samples were placed in a 37 Cwater bath and the pH was adjusted to 8.00 using 0.1 M NaOHand/or 0.1 M HCl, while stirring. Trypsin at a concentration of1.6 mg/ml was maintained in an ice bath and the pH was adjustedto 8.00 with 0.1 M NaOH and/or 0.1 M HCl. Five millilitres ofenzyme solution were then added to the protein suspension, whichwas kept stirred at 37 C. The trypsin had an activity of 13,766BAEE units/mg protein. The pH drop was recorded at 15 s afterenzyme addition and at one minute intervals for 10 min. Theenzyme solution was always freshly prepared before each seriesof experiments. The percent protein digestibility (Y) was calculatedby using Eq. (1) (Hsu et al., 1977):Y ¼ 210:464 18:1x; ð1Þwhere x is the change in pH after 10 min.
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