Abstract
Proteinous lipase inhibitor (LI) from wheat flour was purified to homogeneity using hydrophobic chromatography, gel chromatography, affinity chromatography, SDS-PAGE, and two-dimensional electrophoresis. Molecular masses of the LIs were approximately 28 and 25 kDa as estimated by SDS-PAGE. The amino acid sequences from the N termini of the three components detected by two-dimensional electrophoresis were Arg-Ser-Ala-His-Glu-Pro-Gln-Gln-Pro in the two 25 kDa isolates and Arg-Ser-Ala-His-Glu-Glu-Gln-Gln-His in the 28 kDa isolate, and they were suggested to be genetic variants. The LI was activated by the heating procedure up to 80 o C and stable in the pH range from 3.0 to 7.0
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