Safety Assessment of Novel Foods and Food Proteins

Authors

Niloofar Moghadam Maragheh, University of Nebraska-LincolnFollow

First Advisor

Richard E. Goodman

Date of this Version

Fall 11-2022

Document Type

Article

Comments

A THESIS Presented to the Faculty of The Graduate College at the University of Nebraska In Partial Fulfillment of Requirements For the Degree of Master of Science, Major: Food Science and Technology, Under the Supervision of Professor Richard E. Goodman. Lincoln, Nebraska: November 2022

Copyright © 2022 Niloofar Moghadam Maragheh

Abstract

The global food market needs to grow and supply food demand to feed the growing world population. Alternative food proteins, including novel sources of safe foods and ingredients, are the candidates that could provide more environmentally sustainable choices, animal welfare, and consumers health. Novel foods and food proteins must undergo premarket safety evaluations including allergenicity assessment to reduce the risk of cross-reactivity with known allergens and uncharacterized risk to food allergic individuals. This research addressed the safety assessment of some novel foods and food ingredients using the study of stability of proteins in pepsin and sequence identity analysis in the AllergenOnline database. Subject samples included microalgae, hemp heart protein, sweet protein, and manganese related peroxidase.

In addition, food allergy is a complicated and multifactorial disease. Safety evaluation based on the IgE binding, as a part of risk assessments required by CODEX for the protein sequence identity matches of >35%, usually overestimates the true cross-reactivity due to the false positive results. The results of this study revealed that in vitro protein stability in pepsin in conjunction with other safety assessments can suggest a positive predictive value for a putative food allergen.

The proposed approach described in this thesis included a combination of assays of protein stability in pepsin and meaningful sequence identity matches. Serum IgE binding evaluations would be useful when the match criteria are >50% sequence identity in a full sequence. For the biological relevance of these assessments, serum inhibition western blot analysis and basophil activation test (BAT) using humanized rat basophilic (hRBL) cell line can improve the accuracy of food safety assessment for the risk of novel food proteins. The combination of all methods used in this study would help to propose a better approach for food security and premarket evaluations of novel food proteins.

Advisor: Richard E. Goodman