Use of Enzymes for the Separation of Protein from Rice Flour

When rice flour was treated with heat stable α-amylases, the effectiveness of protein separation increased with increased temperature. Depending on the enzyme, treatment at 90°C for 45 min resulted in protein contents of 47–65% for the insoluble fraction. Prior gelatinization enhanced the effectiveness of the enzyme reaction but was undesirable because the increased viscosity and gelation could cause difficulties in the processing operation. Follow-up treatment with other carbohydratehydrolyzing enzymes, such as glucoamylase, cellulase, and hemicellulase further increased the protein content up to 76% for the insoluble fraction. The subunit structure of the isolated proteins, based on electrophoretic analysis, remained practically unchanged after the treatment. The limited solubility and emulsion activity of rice protein were also unchanged.     

Light-Scattering Molecular Weights and Intrinsic Viscosities of Processed Waxy Maize Starches in 90% Dimethyl Sulfoxide and H2O

Waxy maize starch was treated by a variety of gentle and severe methods: direct dispersion-solubilization into 90% dimethyl sulfoxide (DMSO) and H₂O solvent, extrusion followed by dispersion-solubilization of the ground exudate into solvent, or jet-cooking or stirred autoclaving of an aqueous starch slurry followed by transfer into solvent. Intrinsic viscosities [η] and multiangle light-scattering measurements were made in 90% DMSO-H₂O. A Mark-Houwink relation, [η] = (0.28–1.2) M_w^{0.29 ± 0.04}, was obtained over a molecular weight range of ≈30–700 million. However, there was a large amount of scatter in the data when [η] were >140 mL/g. The power law relationship R_g ∝ M_w^0.41±0.04 was noted between radii of gyration and molecular weights. We infer from our data that over the entire range of M_w distributions, the amylopectin existed in solution as relatively compact molecules or aggregates and that in the higher molecular weight region, the size and possibly the shape of the “dissolved” amylopectin was highly sensitive to the method of dispersal and treatment.