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dc.contributor.advisorCook, Mark E.
dc.contributor.authorBobeck, Elizabeth A.
dc.date.accessioned2007-05-25T17:47:40Z
dc.date.available2007-05-25T17:47:40Z
dc.date.issued2007
dc.identifier.urihttp://digital.library.wisc.edu/1793/8150
dc.description59 p.en
dc.description.abstractNutritionally and economically-important heat-labile proteins, including enzymes, hormones, and antibodies (Ab), lose a substantial amount of activity following industrial processing. Protection of these heat-sensitive bioactive molecules is needed in order to realize expanded markets for these biologics. Using a model of heat-labile proteins, Ab to phospholipase A2, and a sensitive detection system for Ab binding (ELISA), a pilot steam chamber was designed and constructed to develop methods of encapsulating proteins. After modification of the pilot chamber, it was shown that water plays a key role in Ab destruction. Samples (Ab, trehalose-encapsulated Ab, and industry standard) dried with drierite before steam treatment retained 100% activity after 60 seconds in 92-93C in a sealed 15ml centrifuge tube, while samples not dried but sealed prior to steam treatment lost activity (Ab retained 72.24% activity, trehalose-encapsulated Ab retained 74.03% activity, and industry standard retained 42.26% activity). A hydrophobic protein matrix (HPM) was developed. 41.73% binding activity remained in 1% Ab in pasta matrix, 0.94% remained in Ab in egg matrix, and 4.5% remained in industry standard after 60s in 92-93C in unsealed containers. This RPM may protect against steam-induced losses by protecting Ab from water.en
dc.format.extent931690 bytes
dc.format.mimetypeapplication/pdf
dc.language.isoenen
dc.subjectBiologyen
dc.subjectAnimal Sciencesen
dc.titleStudies on the heat stability of egg yolk antibody (lgY)en
dc.title.alternativeStudies on the heat stability of heat-labile proteinsen
dc.typeThesisen


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