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Defatted banana peel powder was fractionated using the Osborne method to extract albumin, globulin, prolamin, and glutelin for physicochemical and functional characterization. The total recovery of protein was ∼89.76%. Albumin was the dominant one in terms of yield (62.4%) and protein content (65.15%) among all the fractions. The mean diameter of albumin (635.05 µm) and glutelin (642.62 µm) were significantly smaller than globulin (726.81 µm) and prolamin (986.45 µm). The highest water (1.86 ± 0.12 g/g), oil (1.97 ± 0.12 g/g) holding capacity, and emulsion capacity (59.27 ± 1.25%) were found for the albumin fraction. In contrast, the glutelin fraction showed the highest foaming capacity (19.13 ± 0.41%) and dispersibility (951.55 ± 3.83 g/kg). The denaturation temperature of protein fractions was found in the range of 30.31-82.08 °C. FTIR confirmed low carbohydrates and protein richness of albumin fraction. XRD revealed the crystalline nature of albumin (65%) and the amorphous nature of other fractions (41-45%). The morphology of all fractions was different, which influenced the functional characteristics.
Deb et al. (Wed,) studied this question.