Derek Dee

Assistant Professor

Research Interests

Agri-food Transformation Products
aspartic proteases
Biological and Biochemical Mechanisms
Enzymes and Proteins
food chemistry
food proteins
funtional amyloid
meat analogues
Nutriceuticals and Functional Foods
protein aggregation
protein engineering
Protein Folding
protein nanofibrils
psychrophilic enzymes

Relevant Thesis-Based Degree Programs


Research Methodology

bioconjugate chemistry
non-standard amino acids
optical tweezers
neutron scattering


Master's students
Doctoral students
Postdoctoral Fellows
Any time / year round

1. genetic and chemical modification to engineer functional amyloid

2. examine misfolding and aggregation of prion proteins

3. conversion of plant proteins into nanofibrils for use in foods

4. mechanisms of biofilm-associated amyloid fibril formation

I support public scholarship, e.g. through the Public Scholars Initiative, and am available to supervise students and Postdocs interested in collaborating with external partners as part of their research.
I support experiential learning experiences, such as internships and work placements, for my graduate students and Postdocs.
I am open to hosting Visiting International Research Students (non-degree, up to 12 months).
I am interested in hiring Co-op students for research placements.

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Graduate Student Supervision

Master's Student Supervision

Theses completed in 2010 or later are listed below. Please note that there is a 6-12 month delay to add the latest theses.

Formation and characterization of legume protein amyloid fibrils (2022)

Amyloid fibrils are gaining attention as novel food ingredients and nanomaterials, due to their unique structural and chemical properties, and functionality as stabilizers and gelling agents. Amyloid fibrils are long, thin, unbranched protein aggregates that are important in medicine, biology and nanotechnology. Many proteins, including food proteins (e.g., from milk, eggs, and legumes), can be converted into amyloid fibrils under the proper conditions, most commonly by heating at low pH. Most of the research on nanofibrils has dealt with animal proteins, so a fundamental understanding of the self-assembly, structure, and functionality of nanofibrils derived from plant proteins is lacking. Plant protein is considered a sustainable source of protein. However, the functional properties of plant proteins, such as foaming, gelling, and emulsification, are generally inferior to that of animal proteins. Consequently, one method to improve the functionality of plant proteins is to produce nanofibrils, which are promising materials.The goal of this research was to relate nanofibril structure and functionality by comparing nanofibrils made from various legume proteins. Nanofibrils were formed from peanut, lentil, pea, and mung bean during incubation at pH 2 and 85 °C. The results showed that protein extracts from peanut, mung bean, pea, and lentil formed nanofibrils, which were detected using thioflavin T and transmission electron microscopy (TEM). SDS-PAGE revealed that extensive protein hydrolysis occurred during the onset of fibril formation, indicating the significance of hydrolysis to fibrillation under these conditions. Using TEM, fibrils from different legumes showed morphological variability with differences in length, width, and flexibility. This research revealed that peanut, lentil, and mung bean fibrils were most soluble at pH 2 and least soluble at isoelectric point (pI) pH. Also, the fibrils showed smaller particle size at pH 2 to that of pH 7 which is consistent with the solubility result. The presence of the fibrils results in an increase in viscosity compared to the unheated samples. The findings showed that a better understanding of legume fibrils is needed to increase their usage as functional materials in food systems, and that this would probably extend theoretical knowledge of the structure-function relationship between plant-based fibrils.

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