| dc.contributor.advisor |
Cook, Mark E. |
|
| dc.contributor.author |
Bobeck, Elizabeth A. |
|
| dc.date.accessioned |
2007-05-25T17:47:40Z |
|
| dc.date.available |
2007-05-25T17:47:40Z |
|
| dc.date.issued |
2007 |
|
| dc.identifier.uri |
http://digital.library.wisc.edu/1793/8150 |
|
| dc.description |
59 p. |
en |
| dc.description.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. |
en |
| dc.description.provenance |
Submitted by Beverly Phillips (bphillips@library.wisc.edu) on 2007-05-25T17:40:53Z
No. of bitstreams: 1
2007_Bobeck.pdf: 931690 bytes, checksum: 9624a77c15618046f88c7d7fba56b6d6 (MD5) |
en |
| dc.description.provenance |
Approved for entry into archive by Beverly Phillips(bphillips@library.wisc.edu) on 2007-05-25T17:47:40Z (GMT) No. of bitstreams: 1
2007_Bobeck.pdf: 931690 bytes, checksum: 9624a77c15618046f88c7d7fba56b6d6 (MD5) |
en |
| dc.description.provenance |
Made available in DSpace on 2007-05-25T17:47:40Z (GMT). No. of bitstreams: 1
2007_Bobeck.pdf: 931690 bytes, checksum: 9624a77c15618046f88c7d7fba56b6d6 (MD5) |
en |
| dc.format.extent |
931690 bytes |
|
| dc.format.mimetype |
application/pdf |
|
| dc.language.iso |
en |
en |
| dc.subject |
Biology |
en |
| dc.subject |
Animal Sciences |
en |
| dc.title |
Studies on the heat stability of egg yolk antibody (lgY) |
en |
| dc.title.alternative |
Studies on the heat stability of heat-labile proteins |
en |
| dc.type |
Thesis |
en |
