Witches as Political Criminals: Prosecution and Deportation in Colonial Kenya

From the Washington University Senior Honors Thesis Abstracts (WUSHTA), Spring 2018. Published by the Office of Undergraduate Research. Joy Zalis Kiefer, Director of Undergraduate Research and Associate Dean in the College of Arts & Sciences; Lindsey Paunovich, Editor; Helen Human, Programs Manager and Assistant Dean in the College of Arts and Sciences Mentor: Timothy Parson

Follow-up of College of Agriculture Graduates at Oklahoma State University: 1979-1983

Agricultural Educatio

Galacto-Oligosaccharides : production, properties, applications, and significance as prebiotics

Galacto-oligosaccharides (GOS) have now been definitely established as prebiotic ingredients after in vitro and animal and human in vivo studies. Currently, GOS are produced by glycoside hydrolases (GH) using lactose as substrate. Converting lactose into GOS by GH results in mixtures containing GOS of different degrees of polymerization (DP), unreacted lactose, and monomeric sugars (glucose and galactose). Recent and future developments in the production of GOS aim at delivering purer and more efficient mixtures. To produce high-GOS-content mixtures, GH should not only have good ability to catalyze the transgalactosylation reaction relative to hydrolysis, but also have low affinity for the GOS formed relative to the affinity for lactose. In this article, several microbial GH, proposed for the synthesis of GOS, are hierarchized according to the referred performance indicators. In addition, strategies for process improvement are discussed. Besides the differences in purity of GOS mixtures, differences in the position of the glycosidic linkages occur, because different enzymes have different regiochemical selectivity. Depending on oligosaccharide composition, GOS products will vary in terms of prebiotic activity, as well as other physiological effects. This review focuses on GOS production from synthesis to purification processes. Physicochemical characteristics, physiological effects, and applications of these prebiotic ingredients are summarized. Regulatory aspects of GOS-containing food products are also highlighted with emphasis on the current process of health claims evaluation in Europe.Agência da Inovação-Progama IDEIA (Portugal)Fundação para a Ciência e a Tecnologia (FCT

Enzymes in organic synthesis

Typescript (photocopy).Several aspects of the use of enzymes as catalysts in organic synthesis have been explored. The stability of the enzyme glucose dehydrogenase useful in reduced nicotinamide cofactor (NAD(P)H) regeneration has been studied. The enzyme has been found to be much more stable than other enzymes commonly used in NAD(P)H regeneration. The enzyme FMN reductase has been used in oxidized nicotinamide cofactor (NAD(P)H) regeneration. The regeneration system using this enzyme is much faster and more efficient than the nonenzymatic system used previously. The substrate specificity of the enzyme hexokinase has been analyzed with regard to fluorinated analogs of D-glucose and analogs having an amino or thiol group at the five position. The enzyme has been found to accept a wide variety of analogs as substrates although the rates are often quite low. 3-Deoxy-3-fluoro-D-glucose has been converted to the 6-phosphate using hexokinase and ATP and this product has been converted chemically to 2-deoxy-2-fluoro-D-arabinose-5-phosphate. Fructose diphosphate aldolase in combination with glucose isomerase has been used in the synthesis of 6-deoxy-6-fluoro-D-glucose. Fluoro hydroxyacetone phosphate has been found to not be a substrate for aldolase but is a fairly good inhibitor. A seven carbon dideoxy ketose sugar has been synthesized using aldolase catalysis. Also 3,4-¹³C₂-D-glucose has been made from 1-¹³C-glyceraldehyde-3-phosphate using triosephosphate isomerase, fructose diphosphate aldolase and phosphoglucose isomerase as catalysts. Furyl carbinols have been prepared in high optical purity by reduction of the corresponding furyl ketones using the alcohol dehydrogenase from Thermoanaerobium brockii. Racemic furyl methyl carbinol has also been resolved to high optical purity by kinetic resolution using hydrolytic enzymes. Some compounds having low solubility in water have been prepared using enzymatic reductions in biphasic systems. The biphasic system allows the reaction to be carried out in a small reaction volume and reduces product inhibition. The use of arsenate and vanadate to stimulate activity of organic phosphate utilizing enzymes with their unphosphorylated substrate analogs has been studied. Several synthetically useful enzymes have been shown to demonstrate such activity. The utility of this approach to enzymatic synthesis has been demonstrated with the synthesis of a seven carbon sugar using dihydroxyacetone in the presence of arsenate as the substrate instead of dihydroxyacetone phosphate