Fourier Transform Infrared Spectroscopy and Gravimetric Analysis of Protein Denaturation in Egg Albumen Treated with Colocasia Esculenta L. Schott (Taro) Leaf Extract
Document Types
Paper Presentation
School Name
San Beda University-Rizal
Track or Strand
Science, Technology, Engineering, and Mathematics (STEM)
Research Advisor (Last Name, First Name, Middle Initial)
Gigantone Jr., Marcelino G.
Start Date
23-6-2025 1:30 PM
End Date
23-6-2025 3:00 PM
Zoom Link/ Room Assignment
EKR 405
Abstract/Executive Summary
Protein misfolding is one of the leading factors contributing to the development of neurodegenerative diseases. Limited remedies exist, focusing on symptomatic relief, leading to plant-derived compounds gaining attention for their protein-stabilizing potential. The study aims to determine taro leaf extract's effect on egg albumen proteins through infrared spectroscopy to evaluate protein structural change and gravimetric analysis to measure protein denaturation. Four concentrations (12.5, 25, 50, and 100%) were tested against a positive control (diclofenac sodium) and a negative control (distilled water), with all groups containing egg albumen. Significant shifts in the Amide I and II bands revealed lower wavelengths in 100% extract (1630.45 cm⁻¹ and 1539.46 cm⁻¹) compared to diclofenac sodium (1632.92 cm⁻¹ and 1541.58 cm⁻¹) and distilled water (1635.85 cm⁻¹ and 1549.08 cm⁻¹), indicating that 100% had the most structural change of proteins in egg albumen. One-way ANOVA for gravimetric analysis yielded a p-value of 7.11E-05, indicating significance between groups. Tukey's HSD post hoc test showed significance between 100% and concentrations (12, 25, and 50%) with p-values of 0.013, 0.016, and 0.017, suggesting distinct aggregation compared to lower concentrations, and none with controls having p-values of 0.149 and 0.584, reinforcing the extract's coagulative role rather than prevention through an anti-inflammatory effect like diclofenac sodium. Findings suggest that taro leaf extract induces protein structural shifts, conversely to preventing misfolding and promoting stabilization, highlighting its opposite role in protein-protein interactions. Further investigation is needed to explore its broader protein application, providing insights into aggressive misfolding in early-onset neurodegenerative diseases.
Keywords
Fourier Transform Infrared spectroscopy; gravimetric analysis; protein denaturation; protein-protein interactions; taro leaf extract
Research Theme (for Paper Presentation and Poster Presentation submissions only)
Food, Nutrition, and Health (FNH)
Initial Consent for Publication
yes
Statement of Originality
yes
Fourier Transform Infrared Spectroscopy and Gravimetric Analysis of Protein Denaturation in Egg Albumen Treated with Colocasia Esculenta L. Schott (Taro) Leaf Extract
Protein misfolding is one of the leading factors contributing to the development of neurodegenerative diseases. Limited remedies exist, focusing on symptomatic relief, leading to plant-derived compounds gaining attention for their protein-stabilizing potential. The study aims to determine taro leaf extract's effect on egg albumen proteins through infrared spectroscopy to evaluate protein structural change and gravimetric analysis to measure protein denaturation. Four concentrations (12.5, 25, 50, and 100%) were tested against a positive control (diclofenac sodium) and a negative control (distilled water), with all groups containing egg albumen. Significant shifts in the Amide I and II bands revealed lower wavelengths in 100% extract (1630.45 cm⁻¹ and 1539.46 cm⁻¹) compared to diclofenac sodium (1632.92 cm⁻¹ and 1541.58 cm⁻¹) and distilled water (1635.85 cm⁻¹ and 1549.08 cm⁻¹), indicating that 100% had the most structural change of proteins in egg albumen. One-way ANOVA for gravimetric analysis yielded a p-value of 7.11E-05, indicating significance between groups. Tukey's HSD post hoc test showed significance between 100% and concentrations (12, 25, and 50%) with p-values of 0.013, 0.016, and 0.017, suggesting distinct aggregation compared to lower concentrations, and none with controls having p-values of 0.149 and 0.584, reinforcing the extract's coagulative role rather than prevention through an anti-inflammatory effect like diclofenac sodium. Findings suggest that taro leaf extract induces protein structural shifts, conversely to preventing misfolding and promoting stabilization, highlighting its opposite role in protein-protein interactions. Further investigation is needed to explore its broader protein application, providing insights into aggressive misfolding in early-onset neurodegenerative diseases.
https://animorepository.dlsu.edu.ph/conf_shsrescon/2025/paper_fnh/3
