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http://digital.library.wisc.edu/1793/8150
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| Title: | Studies on the heat stability of egg yolk antibody (lgY) |
| Other Titles: | Studies on the heat stability of heat-labile proteins |
| Authors: | Bobeck, Elizabeth A. |
| Advisors: | Cook, Mark E. (Mentor) |
| Keywords: | Biology
Animal Sciences |
| Issue Date: | 2007 |
| 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. |
| URI: | http://digital.library.wisc.edu/1793/8150 |
| Appears in Collections: | Biology Honors Theses and Research Papers
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Files in This Item:
| File |
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Size | Format | Handle |
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| 2007_Bobeck.pdf | | 909Kb | Adobe PDF | http://digital.library.wisc.edu/1793/8151 | View/Open |
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