Physicochemical properties of tilapia (Oreochromis niloticus) actomyosin subjected to high intensity ultrasound in low NaCl concentrations

Tang, Ling; Yongsawatdigul, Jirawat

doi:10.1016/j.ultsonch.2019.104922

Cited by 16 publications

(13 citation statements)

References 34 publications

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“…This phenomenon also revealed that HIU might induce severe destruction of myosin globular head in surimi samples containing higher NaCl contents, which may cause negative effect on surimi gelation. Changes in the remaining Ca 2+ ‐ATPase activity in the surimi pastes are consistent with our previous study in tilapia actomyosin, which also showed that the residual Ca 2+ ‐ATPase activity in 0.2 M NaCl was higher than that in 0.6 M NaCl after HIU treatments (Tang et al., 2020).…”

Section: Resultssupporting

confidence: 91%

“…At present, only a few studies have focused on the application of HIU technology in surimi gelation; HIU can be a promising technology that can improve the surimi gel without the use of chemicals and/or enzymes. Our previous work illustrated HIU‐induced physicochemical changes of fish actomyosin in different NaCl concentrations (Tang et al., 2020). However, how HIU treatment would affect gel properties of fish proteins at various NaCl contents has not yet been elucidated thus far.…”

Section: Introductionmentioning

confidence: 93%

“…Hence, an increase in the soluble myofibrillar proteins and the extent of protein unfolding are expected to lead to strong protein interactions and gel networks. In addition, our previous study suggested a potential use of HIU technology in extraction of actomyosin in low NaCl concentrations (Tang & Yongsawatdigul, 2020). Thus, it is assumed that HIU should positively contribute to the surimi gel under reduced salt concentration due to increased solubility of the myofibrillar proteins, which are thought to be the base element of gel formation.…”

Section: Introductionmentioning

confidence: 99%

“…Thus, it is assumed that HIU should positively contribute to the surimi gel under reduced salt concentration due to increased solubility of the myofibrillar proteins, which are thought to be the base element of gel formation. Nevertheless, myosin globular head might undergo severe conformational changes in high NaCl concentration (0.6 M NaCl) after subjected to HIU treatments (Tang et al., 2020), implying that HIU may not be good for typical surimi gel produced with 2% to 3% NaCl.…”

Section: Introductionmentioning

confidence: 99%

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High‐intensity ultrasound improves threadfin bream surimi gelation at low NaCl contents

Tang

Yongsawatdigul

2021

Journal of Food Science

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Effects of high‐intensity ultrasound (HIU) treatments on gelation of threadfin bream (Nemipterus spp.) surimi at various NaCl contents (0.5, 1, and 2% NaCl) were investigated. Protein extractability at 0.5% NaCl was increased with the ultrasonic intensity (p < 0.05). At all tested NaCl contents, reactive sulfhydryl group (SH) content and surface hydrophobicity of the surimi pastes were increased after HIU treatments and were accompanied by a decrease in the Ca2+‐ATPase activity and total SH content, indicating a greater extent of unfolding and conformational changes induced by HIU at higher NaCl contents. Textural properties and color of the surimi gels at 0.5% NaCl were improved concomitant to an increase in ultrasonic intensity (p < 0.05), whereas HIU treatments resulted in inferior gels at 1 and 2% NaCl. Scanning electron microscopy (SEM) revealed that HIU resulted in a more orderly gel network at 0.5% NaCl. Fourier transform infrared (FT‐IR) spectroscopy indicated that the α‐helix content of the surimi gels was decreased as the ultrasonic intensity and NaCl content increased, confirming that structural changes induced by HIU were more profound at higher NaCl contents. The results suggested that HIU technology can be applied to improve only the 0.5% NaCl surimi gel. Practical Application High‐intensity ultrasound (HIU) improved surimi gel containing 0.5% NaCl due to an increase in protein extractability and protein conformational changes. It is likely to lay a theoretical foundation for utilization of HIU technology in production of surimi‐based products at low/reduced salt levels.

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Section: Resultssupporting

confidence: 91%

Section: Introductionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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High‐intensity ultrasound improves threadfin bream surimi gelation at low NaCl contents

Tang

Yongsawatdigul

2021

Journal of Food Science

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“…As reported by Liu et al [7] , surimi particles (myofibrillar proteins) could act as solid particles to stabilize Pickering emulsions. However, some special features of myofibrillar protein including large molecular weight, poor dispersibility and solubility in water, as well as weak electrostatic repulsions impeded the adsorption of these particles at the two-phase interface and the particle–particle interactions during emulsification [7] , [8] . This further poses a huge challenge to fabricate high-quality myofibrillar protein based-Pickering emulsions, especially with low concentrations of proteins.…”

Section: Introductionmentioning

confidence: 99%

Enhancement of storage stability of surimi particles stabilized novel pickering emulsions: Effect of different sequential ultrasonic processes

Liu

Xia

et al. 2021

Ultrasonics Sonochemistry

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Impact of high hydrostatic pressure on casein micelle‐pea protein systems and comparison with heat treatment

Serrano León,

Gravel,

Perreault

et al. 2024

Sustainable Food Proteins

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Developing mixed systems with both plant‐ and animal‐based proteins is crucial to address the limitations in the techno‐functional properties of plant‐based proteins. While the impact of thermal co‐aggregation on mixed systems has been extensively studied, there is limited information on the effects of non‐thermal processes. Therefore, this study aimed to compare the effects of high hydrostatic pressure (HHP, 600 MPa–5 min) and heat (90°C for 60 min) treatments on the protein profiles in a mixed micellar casein (CN):pea protein (PPI) system, while also elucidating the interactions involved in the formation of protein aggregates. Our results showed that both HHP and heat treatments induced the formation of soluble protein aggregates through disulfide bonds. However, protein aggregation was less prominent after application of HHP. In both treatments, the aggregates primarily consisted of convicilin, vicilin, legumin and lipoxygenase. However, albumin PA2 did not contribute to HHP‐induced aggregates, and vicilin played a lesser role in their formation compared to heat‐induced aggregates. CN from the HHP‐treated CN:PPI sample did not participate in aggregate formation, as previously demonstrated after heat treatment. The presence of residual whey proteins in the CN ingredients explained the formation of CN‐whey protein aggregates after heat treatment and, to a lesser extent, after HHP treatment.

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Physicochemical properties of tilapia (Oreochromis niloticus) actomyosin subjected to high intensity ultrasound in low NaCl concentrations

Cited by 16 publications

References 34 publications

High‐intensity ultrasound improves threadfin bream surimi gelation at low NaCl contents

High‐intensity ultrasound improves threadfin bream surimi gelation at low NaCl contents

Enhancement of storage stability of surimi particles stabilized novel pickering emulsions: Effect of different sequential ultrasonic processes

Impact of high hydrostatic pressure on casein micelle‐pea protein systems and comparison with heat treatment

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