Elaine T. Champagne

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BACKGROUND Because of the widespread use of peanut products, peanut allergenicity is a major health concern in the United States. The effect or effects of thermal processing (roasting) on the allergenic properties of peanut proteins have rarely been addressed. OBJECTIVE We sought to assess the biochemical effects of roasting on the allergenic properties(More)
In rice-consuming countries, specific varieties are recognized as premium, “gold standard” varieties, while others are recognized as being superior but second best, despite being identical using the current suite of tools to evaluate quality. The objectives of this study were to determine if there are distinguishable differences in sensory properties of(More)
A common gastrointestinal tract problem afflicting the elderly is that of reduced hydrochloric acid secretion by the stomach mucosa. This results in raised stomach pH values and in reduced activity of the digestive enzyme pepsin, which is responsible for the hydrolysis of dietary proteins to polypeptides. The effects of these alterations of the stomach on(More)
BACKGROUND The widespread use of peanut products, the severity of the symptoms, and its persistence in afflicted individuals has made peanut allergy a major health concern in western countries such as the United States, United Kingdom, and Canada. In a previous study, the authors showed that the allergenic properties of peanut proteins are enhanced as a(More)
Recently, we have shown that roasted peanuts have a higher level of IgE binding (i.e., potentially more allergenic) than raw peanuts. We hypothesized that this increase in IgE binding of roasted peanuts is due to an increased levels of protein-bound end products or adducts such as advanced glycation end products (AGE), N-(carboxymethyl)lysine (CML),(More)
Phytic acid would form soluble and insoluble complexes with proteins. Our objective was to determine if phytic acid forms insoluble complexes with major peanut allergens, and if such reaction results in a peanut extract with a lower level of soluble allergens and allergenic property. Extracts from raw and roasted peanuts were treated with and without phytic(More)
It is known that peanut allergy is caused by peanut proteins. However, little is known about the impact of roasting on the allergenicity of peanuts. During roasting, proteins react with sugars to form Maillard reaction products, which could affect allergenicity. To determine if the Maillard reaction could convert a nonallergenic peanut protein into a(More)
Peanut allergy is a public health issue. The culprits are the peanut allergens. Reducing the allergenic properties of these allergens or proteins will be beneficial to allergic individuals. In this study, the objective was to determine if peroxidase (POD), which catalyzes protein cross-linking, reduces the allergenic properties of peanut allergens. In the(More)
Polyphenol oxidase (PPO) catalyzes the oxidation of tyrosine residues of proteins and, therefore, their cross-linking. Previously we demonstrated that cross-links produced by peroxidase (POD), which also catalyzes tyrosine oxidation, led to a reduction in the allergenic properties of peanut allergens.11 We postulated in this study that PPO can also reduce(More)
High-oleic peanuts are known for a high content of oleic fatty acid. However, it is not known whether high-oleic peanuts are different from normal chemistry peanuts in levels of allergenicity and end-product adducts (i.e., products cross-linked with proteins). For this purpose, four different peanut cultivars (Florunner, Georgia Green, NC 9, and NC 2) were(More)