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Ultrason Sonochem. 2017 Nov;39:511-519. doi: 10.1016/j.ultsonch.2017.05.026. Epub 2017 May 19.

High intensity ultrasound treatment of protein isolate extracted from dephenolized sunflower meal: Effect on physicochemical and functional properties.

Author information

1
Department of Food Engineering and Technology, SLIET Longowal, Sangrur, Punjab 148106, India. Electronic address: malikfet@gmail.com.
2
Department of Food Engineering and Technology, SLIET Longowal, Sangrur, Punjab 148106, India.

Abstract

The influence of high intensity ultrasound (HIUS) on physicochemical and functional properties of sunflower protein isolates was investigated. Protein solutions (10% w/v) were treated with ultrasound probe (20kHz) and ultrasound bath (40kHz) for 5, 10, 20 and 30min. Thermal stability of protein isolates was reduced as indicated by differential scanning calorimetry. Minimum thermal stability was observed at 20min of sonication and increased further with increase in treatment time indicating aggregation at prolonged sonication. SDS-PAGE profile of proteins showed a significant reduction in molecular weight. Further, surface hydrophobicity and sulfhydryl content increased after HIUS treatment indicating partial unfolding of proteins and reduction in the intermolecular interactions. The particle size analysis showed that HIUS treatment reduced the particle size. Less turbid solution were observed largely due to reduction in particle size. HIUS decreased the available lysine content in protein isolates. Solubility, emulsifying capacity, emulsion stability, foaming capacity, foam stability and oil binding capacity were improved significantly, while as, water binding capacity was decreased. The effect of HIUS on physicochemical and functional properties of sunflower protein isolates was more pronounced in probe sonication rather than bath sonication. Protein isolates with improved functional properties can be obtained using high intensity ultrasound technology.

KEYWORDS:

Functional properties; Particle size; Sunflower protein isolates; Surface hydrophobicity; Ultrasound

PMID:
28732975
DOI:
10.1016/j.ultsonch.2017.05.026
[Indexed for MEDLINE]

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