| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5850215 | Food and Chemical Toxicology | 2015 | 8 Pages |
Abstract
- Allergy-structure relation of tropomyosin Todp1 under high pressure was studied.
- The contents of free sulfhydryl and α-helix decreased with increasing pressure.
- Surface hydrophobility increased at 200 and 400âMPa, but decreased at 600âMPa.
- High pressure enhanced in vitro gastrointestinal protein digestibility.
- 400 and 600âMPa caused more decrease in antigenicity of tropomyosin than 200âMPa.
Keywords
DTNBLC-Q-TOF-MS8-anilino-1-naphthalenesulfonic acidTRISPSMFTBSTHHPSGDDTT5,5′-dithiobis-(2-nitrobenzoic acid)Tris-buffered saline and Tween 20AllergenicityEDTAethylene diamine tetraacetic acidUltravioletsodium dodecyl sulfate-polyacrylamide gel electrophoresisSDS-PAGEphosphate bufferTris(hydroxymethyl)aminomethaneELISAEnzyme-linked immunosorbent assaydithiothreitolcircular dichroismProtein structureANSSimulated gastrointestinal digestionLiquid chromatography quadrupole time-of-flight mass spectrometryHigh hydrostatic pressurePhenylmethanesulfonyl fluorideSurface hydrophobicity
Related Topics
Life Sciences
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Food Science
Authors
Yafang Jin, Yun Deng, Bingjun Qian, Yifeng Zhang, Zhenmin Liu, Yanyun Zhao,