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Material Information
- Title:
- Poster Sessions: Chemistry
- Creator:
- Bailine, Ryan
Boafo, Clara
Brown, Thomas
Burley, Kyle
Burrell, Tanashia
Kearns, Ryan
Kincaid, Warren
Koeppe, Julie
Kuhn, Derek
Pokharel, Namrata
Punzalan, Mikaya
Raymond, Brooke
Roque, Johann
- Publication Date:
- 04/14/2021
- Copyright Date:
- 2021
Notes
- Abstract:
- Determination of Pb in orchard soil samples at the Rice Creek Field Station by Warren Kincaid.
Levels of lead (Pb) in former orchard soils were sampled to determine lead contamination at varying depths below the ground surface. Four sites of Rice Creek Field Station’s abandoned orchard outside of Oswego, NY were sampled with their geographic locations identified. Samples were measured and divided consistently by their depth below the soil surface. Samples were then dried, ground, ashed, and digested for analysis using atomic absorption spectroscopy. Concentrated nitric acid, HNO3, was added to digest and elute the lead from the soil into solution. Use of the insecticide lead arsenate, by orchard farmers of the early and mid1900s-, is likely a main source of this lead being unearthed. Lead typically resides in sandy soils of the O and A horizons. The importance of this investigation into lead contamination is the possible lead exposure to those who visit this now protected nature area as well as to the residents of the surrounding Rice Creek nature area. ( ,,,,,,,,,,,,,,,,,,,,,,, )
- Abstract:
- Analysis of Degradation Pathways for a Biodegradable Plastic by Kyle Burley and Johann Roque.
Stimuli-responsive plastics are materials that are capable of responding to their environment to change their physical properties. These dynamic materials have seen significant growth over the past decade due to their versatility. One field of stimuli-responsive plastics that is of particular interest is degradable plastics. Globally we are facing a plastic waste issue that becomes more detrimental each year. In an effort to develop environmentally-friendly plastics, this research group has developed a stimuli-responsive plastic capable of responding to UV-light, leading to degradation. However, the particular pathway of degradation has yet to be determined. This project focuses specifically on the synthesis of molecular model systems that can be used to determine how our plastic is breaking down in response to light.
- Abstract:
- Investigating the function of enzyme 2O14 by Ryan Bailine and Derek Kuhn.
There are over 3800 structures of unknown function available in the Protein Data Bank (PDB). Of these, we have been working to characterize the enzyme with PDB ID 2O14. Computational analysis indicates that this enzyme is an esterase or lipase, which will hydrolyze ester bonds. We expressed the enzyme in E. coli before isolating the cells by centrifugation and using sonication to break the cell membrane and release the enzyme of interest. We passed the collected supernatant through a Ni-NTA affinity chromatography column to isolate the His-tagged 2O14. We identified which fractions contained 2O14 by using gel electrophoresis (SDS-PAGE) to analyze samples. We then performed a Bradford assay to determine the concentration of the enzyme. To test for the predicted esterase or lipase function, we carried out enzymatic assays using chromogenic substrates. Both the ester substrate, p-nitrophenyl acetate (PNPA), and the lipid substrate, p-nitrophenyl dodecanoate, produce a yellow-colored product when hydrolyzed. In order to test the lipid substrate, we must include detergent in the assay buffer. For this reason, we are also testing hydrolysis of the PNPA substrate in the presence and absence of detergent to understand the effect of the detergent on the enzymatic activity of 2O14.
- Abstract:
- Quantitative Analysis of Diphenhydramine Using Dispersive Liquid-Liquid Microexctraction (DLLME) Paired with GC-MS by Ryan Kearns.
Drug-facilitated crimes (DFC) have been an age-old practice, however over the past three decades the prevalence of DFC has increased to the point of public concern. Recently, a common over-the counter drug diphenhydramine (DPH) has become commonly used as a date rape drug. DPH is highly potent with a short half-life making detection difficult abruptly after a drugging occurs. This work is concerned with the refinement of a dispersive liquid-liquid microextraction (DLLME) method of DPH and other antihistamines from aqueous solution. Gas chromatography coupled with mass spectroscopy (GC-MS) is used for analysis in order to detect DPH in parts per billion (ppb) concentrations. Aqueous solutions of DPH were prepared in a range between 0.005-2 mg/L. Buffered aqueous solutions were spiked using 1mL of a 13:40 ratio of a mixture of acetone and toluene used as dispersive solvent and extraction solvent, respectively. Utilizing liquid nitrogen, the aqueous layer was frozen, and the toluene layer was collected. To increase extraction recovery, a second extraction was performed. The collected toluene layers were evaporated and reconstituted using MeOH, then analyzed by GC-MS. Standard calibration solutions of DPH were prepared and analyzed by GC-MS, and extraction recoveries were calculated.
- Abstract:
- Prediction of Function for Enzyme 4Q7Q by Tanashia Burrell and Mikaya Punzalan.
The goal of our project is to determine the function of an enzyme for which the three-dimensional structure is already known. According to the Protein Data Bank (PDB), 4Q7Q is the crystal structure of a possible lipase from Chitinophaga pinensis. Computational sequence and structure alignments were used to predict the function and determine where the active site is in the 4Q7Q structure. We then expressed this enzyme in E. coli before isolating the cells by centrifugation and using sonication to break the cell membranes and release the enzyme of interest. We passed the collected supernatant through a Ni-NTA affinity chromatography column to isolate the His-tagged 4Q7Q. We used gel electrophoresis (SDS-PAGE) to analyze samples from the column in order to determine which of these contained our target enzyme. The Bradford assay technique was usedAnalysis of to determine the concentration of the enzyme 4Q7Q. Chromogenic substrates were used for the enzymatic assays so that the function of esterase or lipase could be determined. We have demonstrated that 4Q7Q can hydrolyze p-nitrophenyl acetate, which supports its function as an esterase. We are using two different lipid substrates, p-nitrophenyl decanoate and p-nitrophenyl dodecanoate to test for lipase function. We are comparing the activity of 4Q7Q as a lipase using either bile salts or phospholipid vesicles to solubilize the lipid substrates.
- Abstract:
- Analysis of Processed Oats by Using Infrared Analysis by Clara Boafo.
The objective of the project was to find out the variability in food processing by measuring moisture, test weight, outliers, and protein DM in oats. The oats stated above was tested to assess if protein DM strays from one another. The results gained from the GAC 2500 UGMA Machine showed that the test weight all fell within the range of 10-13%, the test weight of 29, 30 and 57 lbs/bu. According to the Infratec Analysis Machine the protein DM was around 14% and the moisture was approximately 10%.
- Abstract:
- Cortisol Measurements in Animals by Brooke Raymond.
Cortisol levels have been studied in various species to understand chronic stress and other health-related factors in domestic and wild animals. Samples such as blood, urine, feces, hair, and nails have been collected from animals to quantify their cortisol levels. Some of these samples have proven difficult to obtain and some cause further stress on the animal. In a collaborative project with the Veterinary College at Long Island University, cortisol levels were quantified in 35 domestic animals, where two different samples in each animal were collected (N=70). Samples were mechanically disrupted, and cortisol was extracted from each. An overnight in methanol extraction was followed up by a 5-minute acetone wash. The process was repeated over two more nights to increase yields. Samples were dried under nitrogen, dissolved in a buffer, and cortisol was quantified using an antibody-based assay called ELISA. The results showed a difference between the cortisol levels in the two types of samples collected. Applications of these sample collection and extraction methods in veterinary medicine could lead to a better understanding of chronic stress and other health-related factors in domestic animals.
- Abstract:
- Testing for esterase function in the enzyme with PDB ID 4Q7Q by Namrata Pokharel.
Enzymes are vital for life and all of life can be explained and better understood through enzymatic studies. The purpose of this project is to study and predict the function of an enzyme by using computational analysis and enzyme kinetics. Among the numerous enzymes of unknown function the enzyme we are working with is a possible lipase from Chitinophaga pinensis DSM 2588 with the PDB ID 4Q7Q. We have expressed this enzyme in E.coli and purified it with the help of Ni-NTA affinity chromatography. Since protein function is often tied to structure, structural comparisons and studies were done using computational tools. Lipase function was predicted after performing both global and local structure alignments using Dali and ProMOL. This function was supported by sequence alignment data from BLAST and PFam. To test for esterase function, enzymatic assays were carried out using two short chained substrates, p-nitrophenyl acetate (PNPA) and p-nitrophenyl butyrate (PNPB). We will determine whether the enzyme has a preference for a longer or a shorter chain ester-containing molecule by comparing these results to hydrolysis of lipid-like substrates with longer carbon chains. We are in the initial stages of these tests and we hope to duplicate our first set of results which show significant esterase activity with the p-nitrophenyl acetate substrate.
- Summary:
- Session Chair: Julia Koeppe
- Acquisition:
- Collected for SUNY Oswego Institutional Repository by the online self-submittal tool. Submitted by Zach Vickery.
Record Information
- Source Institution:
- SUNY Oswego Institutional Repository
- Holding Location:
- SUNY Oswego
- Rights Management:
- All rights reserved by the source institution.
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