Extraction of Jackfruit seed protein: Structural and functional analysis
Abstract
• Microwave-assisted extraction of jack fruit seed protein was conducted. • SEM indicated uneven, elongated flaky jack fruit seed protein structure • XRD diffractogram indicated amorphous nature of jack fruit seed proteins. • Microwave-assisted extraction increased foaming and emulsifying ability. Jackfruit seeds, a by-product of the tropical fruit processing industry, are a rich protein source, with approximately 7% protein. The amino acids present in jackfruit seeds are histidine, threonine, valine, lysine, isoleucine, leucine, and phenylalanine. The study aimed to isolate the protein from jackfruit seeds and analyse its physicochemical, structural, and functional properties. In this study, the protein was isolated from jackfruit seed flour using acid-alkali precipitation and microwave-assisted extraction at 800W. Protein solubility (81.48%) was improved for microwave-assisted extraction compared to the acid-alkali precipitation method (79.48%). The scanning electron microscope analysis showed compact, aggregated, irregular, and elongated flaky protein structure for microwave-assisted extraction compared to acid-alkali precipitation jackfruit seed protein isolate (JSPI). The differential scanning calorimetry study indicated a higher denaturation temperature for microwave-assisted extraction JSPI (106°C) than acid-alkali precipitation JSPI (95°C). FTIR spectra showed nine bands in the acid-alkali precipitation protein, indicating a more complex structure than the microwave-assisted extraction JSPI (6 bands). The XRD diffractogram showed that both isolated proteins were amorphous. Protein isolated by microwave-assisted extraction exhibited enhanced overall properties, making it better suited for a wide range of food applications.
Fields of Study & Subjects
Proteins in Food Systems
Food Chemistry and Fat Analysis
Polysaccharides Composition and Applications
Publication details
- Journal / source
- Food Chemistry Advances
- Publisher
- Elsevier BV
- Volume
- 10
- Pages
- 101245–101245
- Publication date
- 10 February 2026
- Language
- EN