Fabrication and characterizations of lentil protein gels from fibrillar aggregates and the gelling mechanisms study
Heat-induced aggregation and gelation from lentil protein isolate (LPI) were studied over pH levels (pH 2 – 9), protein concentration (1 – 13%, w/w), and heating time (0.5 – 16 h). The LPI gels were formed from both fibrillar and particulate aggregates at pH 2 and 7, respectively. The gels formed from fibrillar aggregates at pH 2 were transparent and showed homogenous and highly interconnected networks. While lentil protein showed weak gelling capacity, the gels prepared from LPI aggregates possessed good mechanical properties, and the optimized gel demonstrated the compressive strength of 2.37 kPa and the water holding capacity of 80.62%. The gelling mechanism study suggests that the high aspect ratio allowed fibrillar aggregates to build a higher level of structures with positive characteristics along with other attractive interactions including hydrophobic interactions and disulfide bonds to build strong gels. Therefore, this research has developed a new strategy to prepare improved lentil protein gels for food texturization from LPI fibrillar aggregates.