Cereal Chem 63:311-315   |  VIEW ARTICLE
Lipid Binding by Protein Films Heated on Glass Beads and Prime Wheat Starch.

M. Seguchi. Copyright 1986 by the American Association of Cereal Chemists, Inc. 

Heat treatment of glass powder or glass beads coated with bovine serum albumin (BSA) imparted strong oil-binding ability similar to that of heat-treated wheat starch. Heat-treated BSA alone showed strong oil- binding capacity (3.4-3.6 ml oil/g BSA) and almost no solubility in water. Other proteins (ovalbumin, casein, gluten, and soybean protein) also exhibited oil-binding ability after heat treatment, but polysaccharides (soluble starch, konjac glucomannan, cyclodextrin, Sephadex G-50, and pectin) did not. Paper chromatography of 20 amino acids indicated that there was no change in amino acids after heat treatment. No differences were observed in the infrared spectroscopy and X-ray diffraction patterns of nonheated and heated BSA. Heated BSA showed far lower susceptibility to pepsin digestion than nonheated BSA, which would suggest the occurance of conformational changes in BSA by heat treatment.