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Fractionation and Characterization of Ipil-ipil (Leucaena Leucocephala (Lam.) de Wit.) Seed Proteins
Thesis Abstract:
Defatted meal from ipil-ipil seeds was found to contain 34.40 ± 0.13 percent crude protein. Total soluble proteins obtained by Osborne fractionation amounted to 79.79 percent, broken down as follows: 51.74 percent albumins, 13.95 percent globulins, 3.90 percent prolamins, and 10.03 percent glutelins. The residue contained 11.92 percent proteins.
Except for the prolamins, all fractions were characterized for their physio-chemical properties. Solubility test showed that both albumins and globulins were least soluble at pH 7.0. When chromatographed through Sephadex G-150, albumins exhibitied two peaks (MW = 243,700); globulins, two peaks (M= 236,000); and glutelins, three peaks (MW = 100,500). Electrophoretic properties revealed 1 bands for albumins, 8 bands for globulins, and 2 bands for glutelins. Polyacrylamide gel electrophoresis in the presence of sodium dedocyl sulfate resulted in eight zones for albumins (MW = 363,900), nine zones for globulins (MW = 368,000), and three zones for glutelins (MW = 114,500).
Amino acid profile indicated the presence of all essential amino acids. However, the amounts of sulfur containing amino acids and tryptophan were lower than those corresponding to the United Nations Food and Agriculture Organization (FAO) protein pattern.