Functional Properties of Proteins from Lima Bean (Phaseolus lunatus L.) Seeds

Abstract

Functional properties were identified for the total globulin (TG), 7S and 11S fractions of Lima bean (Phaseolus lunatus L.) seeds. The 11S component accounted for 58.3% of TGs and the 7S for 41.7%. Solubility was higher in the 7S fraction, especially at alkaline pHs. Water-holding capacity was similar (3 g water/g sample) in both globulin fractions. Oil-holding capacity was higher in the 11S fraction, which also exhibited better foaming capacity and foam stability than the 7S and TG fractions at alkaline pHs. The TG and 7S fractions exhibited low emulsifying capacity and emulsion stability at different pHs (5, 7 and 9), but the 11S fraction had relatively higher values. In suspension at low concentrations, all fractions exhibited shear-thinning (pseudoplastic) behavior. The studied Lima bean globulin fractions exhibit functional properties which make them potentially apt for use in some industrial food systems.

Effects of sequential enzymatic hydrolysis on structural, bioactive and functional properties of Phaseolus lunatus protein isolate

“…The thermal profile of PI showed endothermic transitions at 96.07 °C and 104.06 °C, which correspond to thermal denaturation of 7S and 11S globulin fractions respectively (total ∆H 12.66 J g -1 ), as reported previously (Chel-Guerrero et al, 2011). Moreover, the hydrolysates showed different values (p < 0.05).…”

“…The polypeptides of 7S and 11S fractions exhibit different susceptibilities to hydrolysis due to their different aggregation forms, caused by structural native conformation of globulins (Kain et al, 2009;Chel-Guerrero et al, 2011). According to Molina & Añon (2001), who investigated hydrolyzed soy, large increases in the intensity of some bands for LH were probably related to hydrolysis of the most exposed areas of the polypeptides.…”

“…The antioxidant activity of EH was higher in comparison to hydrolysates from Flavourzyme (11.55 mM mg -1 protein) and Alcalase (10.09 mM mg -1 protein) of P. vulgaris (Torruco-Uco et al, 2009). The high TEAC value could be due to specific proteolytic activity of endoprotease used to hydrolyze vicilins, which show a more active surface (Chel-Guerrero et al, 2011) and produce mixtures of peptides of different size and amino acid composition. Moreover, the emission spectrum of intrinsic fluorescence of EH was indicative of changes at the level of the tertiary structure of the protein, as well as the exposure at aqueous phase of sequences with one or more amino acid residues of His, Trp, Tyr, Met, Pro, Leu, Ile, Val and Ala (Adebiyi et al, 2009).…”

Functional properties of 8S globulin fractions from 15 mung bean (Vigna radiata (L.) Wilczek) cultivars

“…Water absorption capacity and oil absorption capacity represent the ability of the protein to combine with water and oil and are usually used in foods such as sausages and dairy products to enhance the texture and retain the flavour. The water absorption capacity and oil absorption capacity in the present study were higher than 7S globulins from lima beans (1.5 and 2.3 g g −1 , respectively) (Chel‐Guerrero et al ., ). The varied values of the water absorption capacity may be due to the different protein structure and amount of polar amino acids, while the difference in oil absorption capacity may be due to the variation of nonpolar side chains, which bind the hydrocarbon side chain of oil.…”

Rheological properties and gel strength of Phaseolus lunatus protein/carboxymethylated flamboyant gum systems

“…Besides, the analyses of variance indicated that the variables for the two HMS samples (at 25 °C), which significantly ( P < 0.05) affected the k values, were the ratio of PH/CFG and the pH, thus with some effect on k , as observed in eqns 2 and 3; k values increase with both the ratio of PH/CFG and the pH value. Those changes observed might be explained by the protein molecular conformational changes occurring at alkaline pH values (Betancur‐Ancona et al ., ; Chel‐Guerrero et al ., ).…”