Physicochemical and functional properties of 11S globulin from chan (Hyptis suaveolens L. poit) seeds

Thermal and emulsifying properties of globulins from chan ( Hyptis suaveolens L. Poit) seeds

“…(2013) and Rao (2007) mentioned that the gelation process of globular proteins is the result of three progressive stages: thermal denaturation, production of soluble aggregates, and formation of a network that entraps water and other components. However, in this research, a lower gelation point prior to the denaturation process was found; this concurs with reports on sunflower globulins and amarantin (11S globulin from amaranth) as well as 11S globulin from chan (Carrazco‐Peña et al., 2013; De la Cruz‐Torres et al., 2017; Sánchez & Burgos, 1997). Nevertheless, CG exhibited a T m value of 100.9°C and the onset of the gelation process ( T gel ) was around 80°C.…”

“…On the contrary, the T m of an endothermic transition reflects the disruption of the intermolecular interactions that maintain the tertiary and quaternary conformations of the proteins (Yin et al., 2012). CG exhibit a T m value of 100.9°C, similar to other globulins such as buckwheat, chia, and soybean seeds with a T m around 100°C at pH values of 7–7.6 without NaCl (Sandoval‐Oliveros & Paredes‐López, 2013; Tang, 2007); however, the T m value for CG was higher than the purified 11S globulin from chan, reported as 94.1°C (De la Cruz‐Torres et al., 2017). The difference in T m values of CG and purified 11S globulin can be explained due to the influence of other minor proteins for increasing the number of intermolecular interactions, and therefore, stabilizing the tertiary and quaternary structures of proteins present in CG.…”

“…The Gel reinforcement of CG during cooling may be attributed to the reversible formation of hydrogen bonds and Van der Waals interactions between protein molecules within the gel primary network (Nagano, Mori, & Nishinari, 1994; Shevkani et al., 2015). Gel reinforcement has also been observed in other storage proteins from amaranth, field pea, soybean, and kidney bean protein isolates, and also 11S globulin from chan (De la Cruz‐Torres et al., 2017; Nagano et al., 1994; Shevkani et al., 2015; Shevkani, Singh, Rana, & Kaur, 2014).…”

“…In contrast, T gel (74°C–76°C) of 11S globulin from chan also determined by oscillatory rheology, is lower than that of CG. This fact indicates that the purity degree influences significantly the gelation point (De la Cruz‐Torres et al., 2017). Carrazco‐Peña et al.…”

“…Crude globulins were precipitated with 0%–60% ammonium sulfate (2 hr, 4°C), dialyzed against water (4 hr, 2 changes), and lyophilized. The obtained CG fraction was stored at 4°C until further analysis (De la Cruz‐Torres et al., 2017).…”