No description available.

No description available.

No description available.

A linear distribution isotherm described the sorption/desorption of four phenols on the Pima clay loam soil. The linear distribution coefficients for 2,4-dichlorophenol, 2-chlorophenol, phenol and 2,4,6-trichlorophenol were 3.61, 2.93, 0.87, and 0.79. Ionization of the phenols affected their relative distribution order. Hydrogen bonding of phenols to exposed mineral sites accounted for the greater measured sorption than was predicted. The effect of solid concentration on the distribution of phenols was tested over a 10-fold soil/solution range. When a log transformation was performed on the data, a highly significant inverse relationship existed between the distribution of phenols and the soil/solution ratio. A 3-fold increase in the dissolved organic carbon in solution was associated with the decrease in the distribution coefficient. A 3-fold increase in the fraction organic carbon in the soil occurred when dry sludge solids were added to the Pima soil. A substantial increase in the dissolved organic carbon in solution was associated with the addition of sludge solids to the soil. (Abstract shortened with permission of author.)

Our objective was to investigate the mode of interaction between selected food proteins and phenolic compounds. Bovine serum albumin (BSA), bovine beta-lactoglobulin, and soybean glycinin were used with the following phenolic compounds; 3,4,5-trihydroxybenzoic acid (gallic acid), 3,4-dihydroxy cinnamic acid (caffeic acid), p -hydroxycinnamic acid (courmaric acid), and 5,7-dihydroxy 4-methoxy isoflavone (biochanin A). The interaction was investigated using incubation temperatures of 35°, 45° and 55°C at pH 5, 7 and 9. Native and SDS-polyacrylamide gel electrophoresis (PAGE), differential scanning calorimetry (DSC), and Fourier transform infrared (FTIR) spectroscopy were used to identify protein-phenol interactions. Certain phenolic compounds combined with BSA and prevented protein aggregation. In general, the thermal stability of the proteins increased as a result of interaction with phenolic compounds; the most pronounced effect was observed with beta-lactoglobulin in the presence of gallic acid at pH 7. The interaction of the phenols with the proteins resulted in changes in protein secondary structure. (Abstract shortened by UMI.)

Thesis (doctoral)--München, 1934.

Thesis (doctoral)--München, 1934.

No description available.

Typescript (photocopy). / Digitized by Kansas Correctional Industries

No description available.