Protein hydrophobicity of 42 native and partially denatured milk and soy protein samples was determined fluorometrically by using three probes, 1-anilino-8-naphthalenesulfonate (ANS), cis-parinarate (CPA) and 1,6-diphenyl hexatriene (DPH), and chromatographically by using Phenyl Sepharose CL4B (PSC). PSC and ANS hydrophobicities correlated well to the protein insolubility determined at zero zeta potential, whereas no significant correlation was observed between CPA. hydrophobicity and protein insolubility. When backwards stepwise regression analysis was applied to 189 data of protein insolubility, a significant correlation (P < 0.001) was obtained between PSC hydrophobicity, zeta potential and protein insolubility. It is suggested that the aromatic hydrophobicity, in conjunction with zeta potential, may play a more important role in protein solublity than the aliphatic hydrophobicity.

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The effect of nonenzymatic glycation on the structural changes and gelling properties of hen ovalbumin (OVA) through the Maillard reaction was studied. OVA was incubated at the dry state with a rare ketohexose (D-psicose, Psi) and two alimentary sugars (D-fructose, Fru; D-glucose, Glc) at 55 degrees C and 65% relative humidity. To evaluate the modification of OVA by different reducing sugars during the glycation process, the extent of the Maillard reaction, aggregation processes, structural changes, and gelling behaviors were investigated. Reactivity of Psi with the protein amino groups was much lower than that of both Fru and Glc, whereas Psi induced production of browning and fluorescent substances more strongly than the two alimentary sugars did. Furthermore, OVA showed an increased tendency toward multimeric aggregation upon modifying with Psi through covalent bond. The modified OVAs with reducing sugar were similar to nonglycated control sample in Fourier transform infrared (FT-IR) characteristics, but significantly decreased in intensity of tryptophan-related fluorescence. The results indicate that although glycation brought about similar changes in the secondary structure without great disruption of native structure, its influence on the side chains of protein in tertiary structure could be different. Breaking strength of heat-induced glycated OVA gels with Psi was markedly enhanced by the Maillard reaction. These results suggest that Psi had a strong cross-linking activity with OVA; consequently, the glycated OVA with Psi could improve gelling properties under certain controlled conditions.

generally accepted that the departure from stoichiometry in these systems, with the consequent occurrence of lattice vacancics and imperfections, makes the movement of ions so facile that i t is impossible for either impurities or pores t o build up on the grain boundaries, thus preventing discontinuous grain growth.Contrary t o the work of Iida,' but in agreement with the work 01 N i~h o l s o n , '~ the increase in grain size with sintering time appeared to follow the empirical law G3 = ht.Ceramic and electrical properties and crystal structures of the system Pb(Mgl/,NbP/J03-PbTi03-PbZrOa are described. The system is composed of three crystal phases at room temperature : pseudocubic, tetragonal, and rhombohedral. A high dielectric constant and radial coupling coefficient and low resonant resistance were obtained for the compositions near the morphotropic transformation. The composition P b (Mgl/,Nb~/~)~.?37~Ti~ 437aZr0 1 2 5 0 3 had the lowest temperature coefficient of resonant frequency.

Ovomucoid, an egg protein comprising approximately 10% egg white, was digested using the enzyme pepsin, and fragments were isolated by anion-exchange and reverse phase HPLC. Four distinct fragments were identified by analysis with SDS-PAGE, including three large fragments with molecular weights of around 24, 18, and 14 kDa. N- and C-terminal and amino acid sequencing analyses identified the fragments as V134-C186 (domain 3), V21-A133, and A1-A133 (domain 1+2). Further separation and sequencing of the fraction composed of small peptides, to determine their exact makeup and location in the protein, remained to be carried out and identified a peptide G51-Y73. All four fragments showed IgE-binding activity, as measured by ELISA, using human sera from egg-allergic individuals. Little change in the digestibility of ovomucoid by trypsin and chymotrypsin was observed following digestion with pepsin, indicating that pepsin-digested ovomucoid retains its trypsin (protease) inhibitor activities. Reduced carboxymethylated ovomucoid was prepared, and digestion with pepsin produced significantly more peptides than did the digestion of the native ovomucoid, indicating that the disulfide bonds play a significant role in the digestive resistance of ovomucoid. The reduction of ovomucoid enhanced its digestibility and lower allergenicity of the protein.