pasta made from parboiled flour, almost regardless of the pasta- making process. The minor but significant differences observed between P2 and P3 may be related to the different starch structure in these samples. It has been suggested that sequential starch gela- tinization/retrogradation cycles may result in protein entrapment in an organized starch structure (Cabrera-Chávez et al., 2012).
The nature of the proteins solubilized in the different media from the various pasta samples was investigated by SDS-PAGE. As shown in Figure 1S, buffer-soluble albumins (25, 18, and 16 kDa; Shih, 2004) were present in P1 but absent in P2 and P3, confirming the data in Fig. 5A. Some of the same low-molecular weight species were solubilized by urea in P2 and P3, along with another polypep- tide at 36 kDa, also present in urea extracts of P1 together with bands at high molecular weight (60 and 65 kDa). These bands were absent in urea extracts of P2 and P3, but the one at 60 kDa was present in both samples when extraction with urea was carried out in the presence of disulfide-reducing agents. These latter con- ditions also allowed solubilization of the 18 kDa species, but not of the one at 65 kDa, possibly as a consequence of easier physical entrapment of the latter and larger species into process-modified starch structures, as discussed above.
Supplementary material related to this article found, in the online version, at http://dx.doi.org/10.1016/j.carbpol.2012.11.047.
Thus, the pasta-making process results in almost all pro- teins being linked through hydrophobic interactions. A previous parboiling step on rice flour provides further stabilization of these interactions by intramolecular disulfide bonds, whose formation
seems insensitive to the conditions used for pasta making and apparently involving specific proteins in a preferential way.
Quantification of accessible SH groups, that may be carried out independently of protein solubility, has been applied to under- standing the nature and evaluating the extent of modification induced in cereal-based foods by processing (Cabrera-Chávez et al.,
2012; Elkhalifa et al., 2006; Mariotti et al., 2011). As shown in Fig. 5B, the number of accessible thiols decreased in the order P1 > P2 > P3 both in the absence and in the presence of urea, con- firming the impact of parboiling on the compactness of the protein matrix. The lower content of accessible thiols in P3 vs P2 indi- cates that the effects of extrusion-cooking on protein structure rearrangements are more dramatic than those of conventional extrusion. The relevance of hydrophobic interactions to the com- pactness of the protein matrix is made evident by the increase in accessible thiols upon addition of urea. Altogether, thiol acces- sibility data confirm the fundamental role of the pasta-making process in establishing the compactness of the protein aggregates, as pointed out by the solubility approaches described above.
3.3. Properties of cooked pasta as related to the starting material and the pasta-making process
3.3.1. Physical and chemical properties of cooked pasta
Data summarizing the cooking performance of the various sam- ples of rice pasta are presented in Table 1. Pasta P3, made by extrusion-cooking of flour from previously parboiled rice (PRF), gave the lowest cooking losses and the lowest water absorp- tion, and was by large the most resilient product. The impact
A 60
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