2026-06-29 ジョージア大学
＜関連情報＞
- https://news.uga.edu/could-marigolds-be-the-next-superfood/
- https://pubs.acs.org/doi/10.1021/acsfoodscitech.5c01215
持続可能な食品原料としてのマリーゴールド花タンパク質の構造的、熱的、機能的特性の評価 Assessing Structural, Thermal, and Functional Characteristics of Marigold Flower Protein as a Sustainable Food Ingredient
Fidele Benimana,Nancy Alila,Kentaro Kawata,Christopher Kucha,Anupam Roy,and Anand Mohan
ACS Food Science & Technology Published: April 2, 2026
DOI:https://doi.org/10.1021/acsfoodscitech.5c01215
Abstract
The demand for sustainable and alternative protein sources has been on the rise, driving interest in the valorization of underutilized plants. This study evaluated Calendula officinalis (marigold), a common floral waste, as a sustainable alternative protein source for the food industry. The primary objective of this study was to investigate the physicochemical properties of protein fractions from Calendula officinalis flower to evaluate their potential as a novel protein ingredient. Extraction of the Calendula officinalis flower yielded 9.217 of the crude protein. A sequential extraction of albumin, globulin, glutelin, and prolamin from marigold flower revealed albumin as the dominant fraction (65.47%) and exhibited the highest protein functionality, including water-holding capacity (2.37 g/g), oil-holding capacity (2.49 g/g), and emulsifying capacity (65.22 mL/g). Compared with other protein fractions, glutelin showed a relatively high emulsifying and foaming capacity (EC: 59.13 mL/g; FC: 16.23%). Differential scanning calorimetry revealed high thermal stability for albumin (Tp = 105.28 °C) and glutelin (Tp = 97.6 °C). Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis (SDS-PAGE) and Liquid Chromatography–Mass Spectrometry (LC-MS) confirmed the presence of abundant low-molecular-weight polypeptides (<37 kDa), which enhanced emulsification, while scanning electron microscopy revealed porous structures aligned with hydration properties. Antioxidant activity was higher in albumin and glutelin, linked to surface hydrophobicity. LC-MS/MS identified 33 short-chain proteins, including oxidoreductase proteins and lipid-transfer proteins. Findings highlight marigold flower proteins as a sustainable, functional ingredient for a diverse range of food applications.
