353: Structure, Thermal, and Functional Properties Characterization of Marigold Flower Proteins for Novel Functional Food Development

Introduction

The growing global demand for plant-based proteins is driven by their potential to improve food functionality, enhance nutritional value, and promote environmental sustainability. Marigold flower proteins represent an underutilized plant-derived protein resource with promising applications in the food industry. This research aims to characterize marigold flower protein' functional, thermal, and structural properties and evaluate their potential for use in food products, focusing on antioxidant activity, protein stability, and functional properties critical to food formulation.

Marigold flowers are an underutilized plant for protein source with potential applications in the food industry, their functional, thermal and structural properties were characterized in this research and its potential use in food products evaluated with regard to its antioxidant activity, protein stability and other functional properties essential for food formulation, with a view to improving food functionality, enhancing nutritional value and promoting environmental sustainability in response to growing global demand for plant based proteins.

Methods

The marigold flowers were fractionated into protein fractions using Osborne’s sequential extraction method, classifying proteins into albumin, globulin, prolamin, and glutelin. The amount of protein and the antioxidant activity of the samples were determined using standard biochemical analyses, while the total phenolic content was estimated using the spectrophotometric method. SDS PAGE was employed to determine the protein size, while DSC provided insights into thermal stability. Functional properties such as foaming capacity, water-holding capacity, oil-holding capacity, and emulsifying activity were assessed. Proteomic analysis was conducted to identify and classify proteins present in marigold flower.

Results

Osborne's sequential extraction method yielded a total protein content of 6.32 ± 0.43 g, accounting for 82.30% of crude protein, with glutelin contributing the highest fraction (4.3 ± 0.17 g), Antioxidant activity was highest in prolamin. SDS-PAGE revealed distinct protein sizes for each fraction, and DSC analysis showed that marigold flower protein extract has high thermal stability. Protein Functionality analyses highlighted glutelin's superior foaming and water-holding capacities and albumin's excellent oil-holding and emulsifying properties.

Significance

The findings suggest that Marigold flower proteins hold significant potential for the food industry application, enhancing food quality and offering benefits such as improved nutrient retention, extended shelf life, and acting as natural food preservatives.

Authors: Fidele Benimana, Christopher Kucha, Anupam Roy, Fanbin Kong, Adhikari Koushik, Anand Mohan