## 3 Results and Discussion
### Physico-Chemical Characterization of the Hydrolysates
#### 3.1.2 SDS-PAGE Electrophoretic Pattern  
SDS-PAGE electropherogram of BKI, RKI, and WKI showed in lanes 1, 2, and 3, respectively (Figure 1). Seventeen bands were detected in lanes (1-3) with molecular weights in the range 11-135 kD, referring to similar protein patterns in the three cultivars of kidney beans. Storage proteins, i.e., victim (7S), and phaseolin (8S), were found within the molecular weights between 40-75 kD. The bands representing phaseolin (40-48 kD), seem more intense than those representing victim in accordance with [PERSON], et al. [32], indicating that phaseolin was the most abundant protein of the common bean. These bands  
\begin{table}
\begin{tabular}{c c c c c c c c c c} \hline \hline \multicolumn{1}{c}{**Chemical Composition (\%)**} & \multicolumn{3}{c}{**Black Kidney bean**} & \multicolumn{3}{c}{**Red Kidney bean**} & \multicolumn{3}{c}{**White Kidney bean**} \\ \hline \multicolumn{1}{c}{**Material Status**} & \multicolumn{1}{c}{**T**} & \multicolumn{1}{c}{**I**} & \multicolumn{1}{c}{**H**} & \multicolumn{1}{c}{**T**} & \multicolumn{1}{c}{**I**} & \multicolumn{1}{c}{**H**} & \multicolumn{1}{c}{**T**} & \multicolumn{1}{c}{**I**} & \multicolumn{1}{c}{**H**} \\ \hline \multicolumn{1}{c}{**Protein**} & \(24.5\pm 0.1^{*}\) & \(91\pm 1.1^{*}\) & \(88\pm 0.7^{**\pm}\) & \(22.7\pm 0.7^{**\pm}\) & \(88.9\pm 1.2^{**\pm}\) & \(85\pm 1^{*}\) & \(21.3\pm 0.6^{*}\) & \(85\pm 0.9^{*}\) & \(82\pm 0.6^{**\pm}\) \\ \multicolumn{1}{c}{**Carbohydates**} & \(62.1\pm 0.3^{**\pm}\) & \(32.5\pm 0.4^{*}\) & \(47.0\pm 0.1^{*}\) & \(65.1\pm 0.8^{*}\) & \(36.7\pm 0.8^{**\pm}\) & \(8.7\pm 0.2^{*}\) & \(64.2\pm 0.8^{*}\) & \(372\pm 0.5^{*}\) & \(8.3\pm 0.1^{*}\) \\ \multicolumn{1}{c}{**Fat**} & \(2.1\pm 0.1^{*}\) & ND & ND & \(2.5\pm 0.1^{**\pm}\) & ND & ND & \(3.1\pm 0.1^{*}\) & ND & ND \\ \multicolumn{1}{c}{**Ash**} & \(4.5\pm 0.3^{*}\) & \(64\pm 0.1^{*}\) & \(7.3\pm 0.2^{**\pm}\) & \(41.9\pm 0.2^{*}\) & \(5.7\pm 0.1^{*}\) & \(6.5\pm 0.1^{*}\) & \(5.1\pm 0.2^{*}\) & \(7.2\pm 0.2^{\pm}\) & \(9.4\pm 0.1^{*}\) \\ \multicolumn{1}{c}{**Measure**} & \(5.8\pm 0.1^{*}\) & \(3.1\pm 0.1^{*}\) & ND & \(6.14\pm 0.2^{*}\) & \(3.5\pm 0.1^{*}\) & \(0.88\pm 0.03^{*}\) & \(6.45\pm 0.1^{*}\) & \(1.5\pm 0.01^{*}\) & \(0.98\pm 0.02^{*}\) \\ \hline \hline \end{tabular}  
* ND, not detected. All values are expressed as means \(\pm\) SD; Means with different lowercase letters in the same row indicate significant differences at \(p\leq 0.  
were relatively the least affected by the 30-min Alcalase hydrolysis as manifested in the electrophoretic pattern of BKH, RKH, and WKH in lanes 4, 5, and 6, respectively. Extending the Alcalase hydrolysis time to 60 min led to the disappearance of these bands (data not shown). The observed resistance of phaseolin to enzymatic hydrolysis in the opposite to vicilin, the total disappearance of bands representing 7S (vicilin) but not phaseolin bands, which relatively resisted enzymatic hydrolysis. Likewise, the 42-47 kD bands referring to phaseolin were visualized in SDS-PAGE profiles of black bean protein isolate [70] after 2 h popsin hydrolysis while higher molecular weight bands (>50 kD) disappeared. Similar resistance of phaseolin was noticed after six h popsin hydrolysis of white kidney protein isolate [21]. The observed higher intensity of phaseolin bands in BKH and RKH than WKH might have originated from the higher phenolic content in black and kidney beans, as [PERSON], et al. [71] mentioned.