Thesis (Ph.D.)--Tufts University, 2006. / Submitted to the School of Nutrition Science and Policy. Adviser: William Lockeretz. Includes bibliographical references (leaves 212-232). Access restricted to members of the Tufts University community. Also available via the World Wide Web;

Thesis (M.S.)--University of Alberta, 2009. / "Fall 2009." At head of title: University of Alberta. Title from pdf file main screen (viewed on July 15, 2009). "A thesis submitted to the Faculty of Graduate Studies and Research in partial fulfillment of the requirements for the degree of Master of Science in Agricultural and Resource Economics, Dept. of Rural Economy." Includes bibliographical references.

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3 pp. / Finding foods to bring on a camping or hiking trip may seem challenging. Not only do they need to be nutritious, but they must also leave minimal waste so you can leave the environment just as you found it. Whole foods (such as fruits, nuts, and vegetables) tend to be better choices than processed foods (such as single-use yogurts or pre-packaged cereal bars) since they tend to be rich in nutrients and produce minimal waste. Finding reusable and recyclable ways to package your foods may also help cut down your impact on the environment.

A two part study was designed to investigate radiation-induced structural and nutritional changes in food proteins. Model systems composed of 0.1-10% myoglobin, lactalbumin or BSA were used and the effects of propyl gallate, ascorbic acid, air or nitrogen, pH 5, 6 or 7 citrate or phosphate buffer, and addition of glucose and SDS were investigated. We found that 0.02-0.04% propyl gallate (PG), alone or in conjunction with other solutes, inhibited protein aggregation after irradiation to 0.5 and 1.0 megarad and subsequent -20 C storage for 3-6 months. PG alone at 0.04% yielded up to 90% retention of myoglobin after 0.5 megarad and up to 94% retention of lactalbumin after 1.0 megarad as compared to unirradiated controls. BSA appeared more radiation sensitive than other proteins, and use of 0.02% PG yielded retention of only 10% of the original protein after 1.0 megarad. Use of synergists such as glucose or SDS together with PG allowed up to a two-fold increase in protein retention, while use of 0.02% ascorbic acid led to lower retention compared to samples irradiated alone in control buffer. Irradiations at pH 5 and 6 yielded greater protein retention than at pH 7. Isoelectric focusing of myoglobin revealed acidic shifts in protein pI with new bands at pH 4.9-5.2 after irradiation at pH 6 with glucose and PG. A similar acidic shift was seen in focusing lactalbumin, with major new bands forming at pH 3.7-4.0 after irradiation in pH 6 phosphate with 0.04% PG. BSA showed a bipolar pattern of pI shifts after irradiation in pH 6 phosphate. Mice fed irradiated lactalbumin in factorial studies grew slightly faster and ate more than unirradiated controls, while those fed protein irradiated with 0.02% PG showed slightly decreased rates of gain and feed consumption. Amino acid analysis revealed a 35% decrease in lysine, as compared to control, in diets prepared with protein irradiated to 1.0 megarads in 0.05 M phosphate, pH 6 with 0.02% PG. The negative effects of PG on feeding and growth were reduced when protein was irradiated at 22.5% rather than 15% (w/v). Liver to body weight ratios among animals fed protein irradiated with PG were decreased by 18% in contrast to control animals fed identical, though unirradiated, diet. (Abstract shortened with permission of author.)

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