sciforum-095367: Functionality and structure of protein isolate from decolorized moringa leaf

<p>This study investigated the impact of decolourisation on the functionality and structure of Moringa oleifera leaf powder (MOLP) protein isolate. Decolorization significantly (p ≤ 0.05) changed the proximate composition of MOLP. In general, decolorized MOLP had a higher moisture, ash, and protein content compared to the un-decolorized MOLP (UDMP). Conversely, the fat (4.33%) and carbohydrate (53.75%) contents were higher in the UDMP than in the decolorized MOLP (DMP), which had 0.66% fat and 52.09% carbohydrate. Decolorization significantly influenced the water absorption capacity of the isolate but did not affect its oil absorption capacity. The decolorized protein isolate showed twice the water absorption capacity of the un-decolorized sample, presumably due to differences in the amount of charged and polar amino acids on the surface of the molecule. Scanning electron images revealed that the decolorized protein isolate particles were smaller than those of the un-decolorized isolate. The foaming and emulsion capacities of the isolates were dependent on pH. Glutamic acid and aspartic acid were the major amino acids in both isolates, but decolorization appeared to reduce the total amino acid content in the protein isolate. </p>