Effects of ultrasound-assisted basic electrolyzed water (BEW) extraction on structural and functional properties of Antarctic krill (Euphausia superba) proteins
“…6a. The maximum emission wavelength (λ max ) of untreated krill myo brils (sample A) was 337.5 nm, which is consistent with the ndings of Li et al (2021b). At increasing temperatures, λ max of myo brillar proteins in samples A, B, C, D, and E red-shifted from 337.5 nm to 341.5 nm, which could be linked to the gradual exposure of Trp sides chains to the aqueous solution, thus increasing the polarity of the surrounding environment.…”
Antarctic krill (Euphausia superba) is an important source of biomass and high-quality protein. However, heat treatment of Antarctic krill negatively impacts its quality and compromises its utilization in the food industry. This study aimed to investigate the mechanisms underlying changes in Antarctic krill meat characteristics and physicochemical properties treated at different temperatures and holding times.Findings indicate that at higher temperatures and holding times, hardness and cooking loss of Antarctic krill meat increased dramatically. The low-eld nuclear magnetic resonance (LF-NMR) analysis revealed that the loss of immobile water increased, whereas SDS-PAGE analysis showed that the content of myosin heavy chain decreased signi cantly, and that protein degradation occurred. Fourier transform infrared spectroscopy (FT-IR) and intrinsic uorescence spectra indicated that α-helix motifs were transformed into β-sheets, and that more hydrophobic groups were exposed. The scanning electron microscopy (SEM) results showed that Antarctic krill meat formed corrugated folded regions after heat treatment without forming a three-dimensional water-entrapped structure, which led to signi cant water loss, resulting in rapid deterioration Antarctic krill meat. These results provide the basis for a deeper understanding of processing characteristics of Antarctic krill meat.
“…6a. The maximum emission wavelength (λ max ) of untreated krill myo brils (sample A) was 337.5 nm, which is consistent with the ndings of Li et al (2021b). At increasing temperatures, λ max of myo brillar proteins in samples A, B, C, D, and E red-shifted from 337.5 nm to 341.5 nm, which could be linked to the gradual exposure of Trp sides chains to the aqueous solution, thus increasing the polarity of the surrounding environment.…”
Antarctic krill (Euphausia superba) is an important source of biomass and high-quality protein. However, heat treatment of Antarctic krill negatively impacts its quality and compromises its utilization in the food industry. This study aimed to investigate the mechanisms underlying changes in Antarctic krill meat characteristics and physicochemical properties treated at different temperatures and holding times.Findings indicate that at higher temperatures and holding times, hardness and cooking loss of Antarctic krill meat increased dramatically. The low-eld nuclear magnetic resonance (LF-NMR) analysis revealed that the loss of immobile water increased, whereas SDS-PAGE analysis showed that the content of myosin heavy chain decreased signi cantly, and that protein degradation occurred. Fourier transform infrared spectroscopy (FT-IR) and intrinsic uorescence spectra indicated that α-helix motifs were transformed into β-sheets, and that more hydrophobic groups were exposed. The scanning electron microscopy (SEM) results showed that Antarctic krill meat formed corrugated folded regions after heat treatment without forming a three-dimensional water-entrapped structure, which led to signi cant water loss, resulting in rapid deterioration Antarctic krill meat. These results provide the basis for a deeper understanding of processing characteristics of Antarctic krill meat.
“…Due to the exposure of hydrophobic and polar groups, the contact area of protein and water was increased, which improved its solubility and surface hydrophobicity. However, aggregate occurred among dissociated subunits when the ultrasonic power was over 500 W, which increased the protein particle size, as shown in the red dotted circle [43] . Fig.…”
Highlights
Effect of ultrasound was wholly studied on various protein functions of scallop mantle.
Ultrasound regulated functions by modifying the structure of scallop mantle protein.
Ultrasound can modify structure of scallop mantle protein except primary structure.
“…The results indicated that the ultrasonication promoted the oxhide gelatin to produce a sufficient number of hydrophobic patches to quickly migrate to the air–water interface. After ultrasonication, the oxhide gelatin particles were more evenly dispersed in the solution, which may have increased the FAI [52] .…”
Highlights
Ultrasound increases the DH of gelatin and antioxidant properties of hydrolysate.
Ultrasound facilitates the unfolding of protein structure.
Ultrasound accelerates the thermal degradation of the protein.
Ultrasound changes the morphology and interface characteristics of gelatin particles.
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