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Studies on the heat stability of egg yolk antibody (lgY)

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Author(s)
Bobeck, Elizabeth A.
Advisor(s)
Cook, Mark E.
Date
2007
Subject(s)
Biology; Animal Sciences
Abstract
Nutritionally 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.
Description
59 p.
Permanent link
http://digital.library.wisc.edu/1793/8150 
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