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- All Subjects: Capsaicin
- Creators: Bustamante, Krista Gisselle
- Creators: Owens, Aerial M.
Description
Capsaicin and dihydrocapsaicin account for 90% of capsaicinoids when it comes to the pungency of peppers. Capsaicin stability was investigated through a cooking and storage parameter where three different tests were done; cooking duration, cooking temperature, and storage stability. The concentration of capsaicinoids was quantified through gas chromatography-mass spectrometry where those values were then used to determine the total Scoville heat units (SHU). Furthermore, half-life was determined by finding the decay rate during cooking and storage. Results showed that there was an increase in degradation of capsaicinoids concentration when peppers were cooked for a long period of time. Degradation rate increases with increasing temperatures as would be expected by the Arrhenius equation. Hence, if a maximum pungency is wanted, it is best to cook the least time as possible or add the peppers towards the end of the culinary technique. This would help by cooking the peppers for a short period of time while not being exposed to the high temperature long enough before significant degradation occurs. Lastly, the storage stability results interpreted that a maximum potency of the peppers can be retained in a freezer or refrigerator opposed to an open room temperature environment or exposure from the sun. Furthermore, the stability of peppers has a long shelf life with even that the worse storage condition's half-life value was 113.5 months (9.5 years). Thus, peppers do not need to be bought frequently because its potency will last for several years.
ContributorsBustamante, Krista Gisselle (Author) / Cahill, Thomas (Thesis director) / Sweat, Ken (Committee member) / Armendariz Guajardo, Jose (Committee member) / School of Mathematical and Natural Sciences (Contributor) / Barrett, The Honors College (Contributor)
Created2017-12
Description
Transient Receptor Potential Vanilloid-1 (TRPV1) is an integral membrane polymodal cation channel involved in various essential biological functions, including thermosensing, thermoregulation, and nociception. Discrete TRPV1 activation modes such as ligand, heat, and proton have been challenging to disentangle. However, dissecting the polymodal nature of TRPV1 is essential for therapeutic development. The human TRPV1 (hTRPV1) voltage-sensing like domain (VSLD; transmembrane helices S1-S4) contains the canonical vanilloid ligand binding site and significantly contributes to thermosensing. Nuclear magnetic resonance (NMR)-detected studies probe the role of the hTRPV1-VSLD in TRPV1 polymodal function. The hTRPV1-VSLD is identified as an allosteric hub for all three primary TRPV1 activation modes and demonstrates plasticity in chemical ligand modulation. The presented results underscore molecular features in the VSLD that dictate TRPV1 function, highlighting important considerations for future therapeutic design.
ContributorsOwens, Aerial M. (Author) / Van Horn, Wade D. (Thesis advisor) / Levitus, Marcia (Committee member) / LaBaer, Joshua (Committee member) / Arizona State University (Publisher)
Created2023