Ultrasonication as an innovative approach to tailor the apple seed proteins into nanosize: Effect on protein structural and functional properties
Asir Gani, Zanoor ul Ashraf, Nairah Noor, Idrees Ahmed Wani
Ultrasonics Sonochemistry
Abstract
In this study, protein was extracted from the apple seed flour using alkali-acid precipitation method. The main objective of this study was to evaluate the impact of ultrasonication on structural and techno-functional properties of apple seed protein. Both native (N-protein) and ultra-sonicated protein (US-protein) were characterized for size, zeta potential, structure, protein pattern, crystallinity, thermal stability and functional properties. The results revealed that the hydrodynamic diameter of N-protein and US-protein was 1.2 µm and 484 nm while zeta potential was -11 and -19 mV, respectively. Fourier transform infrared-spectroscopy and X-ray diffraction analysis showed change in the conformational characteristics and functional groups of proteins after nano-reduction. SEM revealed change in the surface morphology of protein molecule upon ultrasonication. Differential scanning calorimetry showed decreased denaturation temperature for US-protein compared to N-protein . SDS-PAGE depicted no change in protein pattern upon ultrasonication. Ultrasonicated protein exhibited increased functional properties like emulsification, foaming, hydrophobicity and oil absorbing properties and hence can be efficiently used as functional ingredient in food and nutraceutical industry.
Extracted Claims
3 claims extracted from this paper into the knowledge graph
ultrasonication increases functional properties emulsification, foaming, hydrophobicity, and oil absorbing properties
“Ultrasonicated protein exhibited increased functional properties like emulsification, foaming, hydrophobicity and oil absorbing properties and hence can be efficiently used as functional ingredient in...”
ultrasonication reduces hydrodynamic diameter from 1.2 µm to 484 nm
“The results revealed that the hydrodynamic diameter of N-protein and US-protein was 1.2 µm and 484 nm while zeta potential was -11 and -19 mV, respectively.”
ultrasonication decreases denaturation temperature of US-protein compared to N-protein
“Differential scanning calorimetry showed decreased denaturation temperature for US-protein compared to N-protein.”