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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

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
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Description
Transient receptor potential vanilloid member 1 (TRPV1) is a membrane protein ion channel that functions as a heat and capsaicin receptor. In addition to activation by hot temperature and vanilloid compounds such as capsaicin, TRPV1 is modulated by various stimuli including acidic pH, endogenous lipids, diverse biological and synthetic chemical

Transient receptor potential vanilloid member 1 (TRPV1) is a membrane protein ion channel that functions as a heat and capsaicin receptor. In addition to activation by hot temperature and vanilloid compounds such as capsaicin, TRPV1 is modulated by various stimuli including acidic pH, endogenous lipids, diverse biological and synthetic chemical ligands, and modulatory proteins. Due to its sensitivity to noxious stimuli such as high temperature and pungent chemicals, there has been significant evidence that TRPV1 participates in a variety of human physiological and pathophysiological pathways, raising the potential of TRPV1 as an attractive therapeutic target. However, the polymodal nature of TRPV1 function has complicated clinical application because the TRPV1 activation mechanisms from different modes have generally been enigmatic. Consequently, tremendous efforts have put into dissecting the mechanisms of different activation modes, but numerous questions remain to be answered.

The studies conducted in this dissertation probed the role of the S1-S4 membrane domain in temperature and ligand activation of human TRPV1. Temperature-dependent solution nuclear magnetic resonance (NMR) spectroscopy for thermodynamic and mechanistic studies of the S1-S4 domain. From these results, a potential temperature sensing mechanism of TRPV1, initiated from the S1-S4 domain, was proposed. Additionally, direct binding of various ligands to the S1-S4 domain were used to ascertain the interaction site and the affinities (Kd) of various ligands to this domain. These results are the first to study the isolated S1-S4 domain of human TRPV1 and many results indicate that the S1-S4 domain is crucial for both temperature-sensing and is the general receptor binding site central to chemical activation.
ContributorsKim, Minjoo (Author) / Van Horn, Wade D (Thesis advisor) / Wang, Xu (Committee member) / Liu, Wei (Committee member) / Arizona State University (Publisher)
Created2019