Ultrasound-assisted extraction of protein from Bombay locusts and its impact on functional and antioxidative properties

Abstract

Impact of ultrasound-assisted process (UAP) on yield, functional properties, antioxidant properties and molecular characteristics of protein extracted from Bombay locusts (BL) (Patanga succinta L.) was studied. Different conditions of UAP were implemented for different amplitudes (40–60%) and times (10–30 min) during aqueous extraction. Notably, UAP could enhance yield and protein recovery, compared with those from typical process (TP) (continuously stirred at 100 rpm at room temperature for 1 h). UAP conditions used governed the change of surface hydrophobicity and free α-amino content of BL. UAP could improve solubility of BL, especially at pH levels higher than 2. UAP had no significant (p > 0.05) detrimental effects on foaming capacity and stability of BL. Nevertheless, UAP, particularly at 50–60% amplitudes, affected the emulsion activity and stability of BL. UAP provided BL with high radical scavenging activities and good electron donating ability, especially that from 60% amplitude for 20 min (UAP-60/20). UAP-60/20 showed the impact on change of isoelectric point and molecular characteristic monitored by Fourier transform infrared (FTIR) of BL, compared to those from TP. In addition, BL was also an excellent source of both essential and nonessential amino acids. Therefore, UAP potentially enhanced BL extraction efficiency, resulting the BL with good functional and antioxidative properties.

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“…An experiment was completed to extract protein from Bombay locusts by implementing ultrasound-assisted extraction. The protein yield from the ultrasound-assisted extraction was significantly higher compared to the typical conventional extraction [89]. This foresees the prospective of LBS integrated with ultrasound-assisted extraction for the recovery of protein as appealing and worthy of further research.…”

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“…These differences in the protein yielding when using PUP may be due to the extraction conditions, the type of ultrasound device and configuration (bath or piezoelectric sonotrode), surface area of the pre-treated samples, residual fat percentage of the powder, and the presence of chitin in the case of Orthoptera ( Choi et al, 2017a ). Moreover, because of the high energy addition to the protein molecules due to ultrasound application, variations on the protein recovery are also attributed to changes in the surface hydrophobicity of proteins, due to splitting and fractionation of the protein structure due to the cavitation phenomenon, which leads to changes in the conformation of the secondary, tertiary, and quaternary structures of the protein, affecting the functional properties such as the solubility ( Kingwascharapong et al, 2021 ). In this sense, proteins in their native state usually perform as aggregates with low dispersibility in aqueous media, but when ultrasound is applied, a large number of cavitation bubbles are produced, which cause a rapid increase in local temperature and pressure at the neiborhood of the collapsing bubbles.…”

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