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Data are the mean + standard deviation of three replicates. Nd: Not determined. Antioxidant and metal chelating activities of fractions purified by Sephadex G10 gel filtration chromatography from the <1 kDa fraction of 210 min protein isolate and phaseolir hydrolysate.

Table 2 Data are the mean + standard deviation of three replicates. Nd: Not determined. Antioxidant and metal chelating activities of fractions purified by Sephadex G10 gel filtration chromatography from the <1 kDa fraction of 210 min protein isolate and phaseolir hydrolysate.

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Fig. 1. Enzymatic hydrolysis of Jamapa bean (Phaseolus vulgaris L.) protein isolate and phaseolin by treatment with pepsin (added at time O min) and pancreatin (added 90 min later). Data correspond to the average + SD of three determinations. Hydrolysis of the protein isolate and purified phaseolin (protein content 88 and 89% w/w, respectively) were carried out by treat- ment with pepsin for 90 min followed by treatment with pancreatin for 120 min as previously reported (Carrasco-Castilla et al., 2012). Degree of hydrolysis (DH) increased up to 16% and 37% for the pro- tein isolate and phaseolin preparations, respectively (Fig. 1). The DH value for the protein isolate hydrolysate was within the range, 12- 34%, previously reported for Azufrado bean protein concentrates that were hydrolysed by treatment with pancreatin for 120 min (Valdez-Ortiz et al., 2012), but was lower than the 26% DH reported for the hydrolysis of protein isolates from hard to cook bean by incubation with pepsin for 90 followed by incubation with pancre- atin for 45 min (Ruiz-Ruiz et al., 2011). These variations are proba- bly due to differences in the methods that were used for protein extraction, or may be also due to differences in protein profile resulting in cultivars more or less susceptible to proteolysis. The variability of beans depends on genetic diversity. Cultivars are clas-
Fig. 1. Enzymatic hydrolysis of Jamapa bean (Phaseolus vulgaris L.) protein isolate and phaseolin by treatment with pepsin (added at time O min) and pancreatin (added 90 min later). Data correspond to the average + SD of three determinations. Hydrolysis of the protein isolate and purified phaseolin (protein content 88 and 89% w/w, respectively) were carried out by treat- ment with pepsin for 90 min followed by treatment with pancreatin for 120 min as previously reported (Carrasco-Castilla et al., 2012). Degree of hydrolysis (DH) increased up to 16% and 37% for the pro- tein isolate and phaseolin preparations, respectively (Fig. 1). The DH value for the protein isolate hydrolysate was within the range, 12- 34%, previously reported for Azufrado bean protein concentrates that were hydrolysed by treatment with pancreatin for 120 min (Valdez-Ortiz et al., 2012), but was lower than the 26% DH reported for the hydrolysis of protein isolates from hard to cook bean by incubation with pepsin for 90 followed by incubation with pancre- atin for 45 min (Ruiz-Ruiz et al., 2011). These variations are proba- bly due to differences in the methods that were used for protein extraction, or may be also due to differences in protein profile resulting in cultivars more or less susceptible to proteolysis. The variability of beans depends on genetic diversity. Cultivars are clas-
Fig. 3. Elution profile of <1 kDa-hydrolysates of protein isolate and phaseolin from P. vulgaris L. var. Jamapa, produced by treatment with pepsin and pancreatin by 210 min, on Sephadex G10 gel filtration chromatography. Bed size, 2.5 x 30 cm; flow rate, 0.5 mL/min; mobile phase, phosphate buffer solution (10 mM, pH 7.4), NaN3 0.02%; fraction size, 2 mL. ‘ig. 2. Electrophoretic (SDS-PAGE) pattern of P. vulgaris protein isolate (a) and yhaseolin (b) hydrolysed with pepsin (added at time 0 min) and pancreatin (added ifter 90 min) at different reaction times. Lane M=MW standards (kDa); Lane =bean protein isolate; Lane P=phaseolin. Protein bands: A: Phaseolin (43- 17 kDa); B: PHA-E, PHA-L (31 kDa); C: Phaseolin 8 type (fragment, 25 kDa); D: -haseolin o type (fragment, 21 kDa), « amylase inhibitor (18 kDa); E: « amylase nhibitor B subunit (15 kDa).
Fig. 3. Elution profile of <1 kDa-hydrolysates of protein isolate and phaseolin from P. vulgaris L. var. Jamapa, produced by treatment with pepsin and pancreatin by 210 min, on Sephadex G10 gel filtration chromatography. Bed size, 2.5 x 30 cm; flow rate, 0.5 mL/min; mobile phase, phosphate buffer solution (10 mM, pH 7.4), NaN3 0.02%; fraction size, 2 mL. ‘ig. 2. Electrophoretic (SDS-PAGE) pattern of P. vulgaris protein isolate (a) and yhaseolin (b) hydrolysed with pepsin (added at time 0 min) and pancreatin (added ifter 90 min) at different reaction times. Lane M=MW standards (kDa); Lane =bean protein isolate; Lane P=phaseolin. Protein bands: A: Phaseolin (43- 17 kDa); B: PHA-E, PHA-L (31 kDa); C: Phaseolin 8 type (fragment, 25 kDa); D: -haseolin o type (fragment, 21 kDa), « amylase inhibitor (18 kDa); E: « amylase nhibitor B subunit (15 kDa).
Data are the mean + standard deviation of two replicates. Nd: Not determined. Amino acid composition (g/100 g protein) of P. vulgaris L protein isolate, phaseolin and their peptidic fractions obtained by gel filtration chromatography Table 2
Data are the mean + standard deviation of two replicates. Nd: Not determined. Amino acid composition (g/100 g protein) of P. vulgaris L protein isolate, phaseolin and their peptidic fractions obtained by gel filtration chromatography Table 2
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