Real-time stability analysis in food systems with magnetic resonance

Date

2024-8

Author

Mercan, Erdem

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Food stability has always been the interest of the consumers, food producers and regulatory authorities. It is becoming more significant due to the food safety and food quality issues. In this thesis, the initial part of the study focused on the development and optimization of a portable NMR probe which will be used to analyze food systems. The design process included simulations to optimize the magnetic field homogeneity and strength. Then, this custom-built portable NMR probe was tested through a model food system which consists of sucrose, corn syrup, gelatine and water. Correlations done through a linear regression model show its use to monitor the total soluble solid content (TSS) and correlated it with T2eff relaxation times. A linear relationship was observed on the plot of data. Regression analysis was performed accordingly. The lack-of-fit test p-value is found to be 0.210 and has a high coefficient of determination (R² = 0.9113) which shows the model fits well. In the second part, to determine if imaging is necessary to fully understand complex food systems, a benchtop Magnetic Resonance Imaging (MRI) was used to assess the food stability in a model food system which is focusing on pea protein isolate (PPI) mixed with high methoxyl pectin (HMP). Particle size measurements showed that for 2% and 4% PPI containing samples, there is a significant increase (p<0.05). Over the 24-hour observation period, T1 weighted image intensity displayed a statistically significant increasing trend (p<0.05). The T2 weighted image intensity shown a significant decrease (p<0.05) since the water molecules' mobility is increasingly restricted, due to the tighter network of protein aggregates limiting the free movement of water protons. On the other hand, T1 and T2 Map showed that the locational T1 and T2 relaxations time are decreasing over the duration.

Subject Keywords

Magnetic resonance, NMR hardware, Aggregation, Pea protein isolates, NMR relaxometry

URI

https://hdl.handle.net/11511/111024

Collections

Graduate School of Natural and Applied Sciences, Thesis