Effects of high-pressure homogenization on functional properties and structure of mussel (Mytilus edulis) myofibrillar proteins

Yu, Chang Yeon; Wu, Fan; Cha, Yue; Zou, Henan; Jie, Bao; Xu, Ruinan; Du, Ming

doi:10.1016/j.ijbiomac.2018.06.134

Cited by 78 publications

(26 citation statements)

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“…Furthermore, researchers have reported that shear action could induce structural changes to various kinds of proteins (e.g. wheat protein, pea protein and chicken breast myofibrillar proteins), resulting in improved functionalities including gel strength, water solubility, forming emulsifying properties, etc . Accordingly the improvement of texture by shearing might be due to the increased disruption of myofibril ultrastructure and protein dispersion in the comminuted surimi paste, and the increased extent of protein unfolding as well .…”

Section: Resultsmentioning

confidence: 99%

“…During the comminution process, ultrastructure of fish muscle is disrupted by salting along with mechanical forces, resulting in the enhanced hydration of myofibrillar proteins . As is well known, homogenization possesses the ability to disrupt the ultrastructure of muscle fiber and disperse the myofibrillar proteins in solution by the mean of shearing mainly, and thus is widely applied for assisting the extraction of intracellular myofibrillar proteins from muscles of various resources . Furthermore, it has been reported that shearing induced structural changes of proteins, like wheat protein, pea protein and chicken breast myofibrillar proteins .…”

Section: Introductionmentioning

confidence: 99%

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Gelling properties of silver carp surimi as affected by different comminution methods: blending and shearing

Liu

Shi

et al. 2019

J Sci Food Agric

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BACKGROUND Blending and shearing, two types of comminution methods, are widely used in the manufacturing of surimi‐based products. The comminution methods applied are varied to product types and manufacturers. In this study effects of different comminution methods (blending and shearing) on gelling properties of silver carp surimi were investigated. RESULTS Regardless of comminution methods, breaking force, penetration distance and water holding capacity of surimi gel significantly increased with comminution duration up to 10 min. As compared with blending, those values under shearing of the same duration were significantly higher. Within 3 min of comminuting whiteness values of gels by shearing were significantly higher than those by blending. Electrophoresis studies showed that comminution method had no obvious effect on protein patterns. Scanning electron microscopy images revealed that more uniform and denser network was formed in the surimi gels made by shearing. Water distribution of the gels made by shearing was obviously more uniform according to magnetic resonance imaging analysis. CONCLUSION Our results suggested that with respect to blending, shearing was a better choice to maximize the gelling ability of silver carp surimi, which resulted in the higher values of texture, whiteness and water holding capacity. It could be attributed to the denser three‐dimensional network and more uniform water distribution of the surimi gel prepared by shearing. © 2019 Society of Chemical Industry

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Gelling properties of silver carp surimi as affected by different comminution methods: blending and shearing

Liu

Shi

et al. 2019

J Sci Food Agric

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“…The increase in EAI and ESI might also be due to the decrease in particle size of MP and fat, leading to an increase in protein adsorption (Table ). The studies of Yu et al . and Chen et al .…”

Section: Resultsmentioning

confidence: 99%

“…found the agglomerated protein after homogenizing MP with a high pressure of 20 000 psi. Other studies also pointed out that high homogenization pressure may cause protein particles to aggregate …”

Section: Resultsmentioning

confidence: 99%

Effects of high‐speed shear homogenization on the emulsifying and structural properties of myofibrillar protein under low‐fat conditions

et al. 2019

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BACKGROUND Emulsification is important for food quality and processing functionality. Most emulsification occurs under high‐fat conditions that eventually cause health concerns. Protein emulsifiers also have drawbacks such as lower dispersity. This study considered the effects of different high‐speed shear homogenization (HSH) speeds on the emulsifying and structural properties of myofibrillar proteins (MPs) under low‐fat conditions. RESULTS High‐speed shear homogenization significantly increased the emulsifying activity and emulsifying stability of MPs at lower speeds (8000 to 14 500 rpm). The primary structure of MP was not altered significantly by HSH, whereas its secondary, tertiary, and quaternary structures were changed. Particle size decreased first and then increased significantly, and reached a minimum when the HSH speed was 14 500 rpm. The absolute zeta potential values increased significantly and the dendritic fibrous structure of sample was destroyed when the speed exceeded 14 500 rpm. High‐speed shear homogenization (14 500 rpm) decreased the particle size and unfolded the protein, which improved the emulsifying properties of MPs. Excessive HSH speeds (20 500 rpm or higher) caused an aggregation of MP molecules, which was not conducive to improving their emulsifying properties. CONCLUSION Optimal HSH speed was achieved at 14 500 rpm to modify MPs' emulsifying and structural properties under low‐fatconditions. © 2019 Society of Chemical Industry

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“…Cavitation, shear, turbulence, and temperature rise affect protein conformational structure, thereby modifying the functionalities (Dumay et al, ; Ye & Harte, ). It has been reported that HPH was performed to modify structural and functionalities of various proteins including dairy proteins (Ali et al, ; Iordache & Jelen, ; Lee, Lefèvre, Subirade, & Paquin, ; Ye & Harte, ), plant proteins (Dong et al, ; Liu & Kuo, ; Song, Zhou, Fu, Chen, & Wu, ; Sun, Dai, Liu, & Gao, ; Yang, Liu, Zeng, & Chen, ), meat proteins (Saricaoglu, Gul, Tural, & Turhan, ) and our previous findings in shellfish proteins (Yu, Cha et al, ; Yu, Wu, Cha, Qin, & Du, ; Yu, Wu, Cha, Zou et al, ). It has also been reported that HPH treatment has potential application for improving the functionality of muscle proteins in water to develop new meat‐based products in food industry (Chen, Xu, & Zhou, ; Chen, Zhou, Xu, Zhou, & Liu, ).…”

Section: Introductionmentioning

confidence: 99%

Structure and functionalities changes in high-pressure homogenized clam protein isolate

Cha

Zou

et al. 2018

J Food Process Preserv

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High‐pressure homogenization (HPH) under 0–100 MPa was performed to treat clam protein isolate (CPI) for three cycles. Results indicated that HPH treatment resulted in significant improvements of CPI functional properties. Absolute zeta potential, emulsifying activity index, and emulsion stability index significantly increased by 19.37 mV, 33.26 m2/g, and 14.00 min after HPH under 100 MPa. Solubility of CPI dramatically increased by 70.8% under 80 MPa. Foaming ability and foaming stability increased by 33.8% and 14.4% under 60 MPa. HPH resulted in significant decrease in percentage of both α‐helix and β‐turn, but percentage of β‐sheet greatly improved as the pressure increased. Free sulfhydryl and surface hydrophobicity increased but fluorescence intensity decreased significantly after HPH treatment. Improvements of these functionalities were due to protein structure changes and particle size reduction. This study demonstrated that HPH has the potential to improve functional properties of shellfish protein through modifying protein structure. Practical applications A nonthermal processing technique using HPH can improve functional properties of CPI, including solubility, emulsifying properties, and foaming properties. Therefore, HPH can be potentially used to process shellfish proteins to improve their functional properties.

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Effects of high-pressure homogenization on functional properties and structure of mussel (Mytilus edulis) myofibrillar proteins

Cited by 78 publications

References 50 publications

Gelling properties of silver carp surimi as affected by different comminution methods: blending and shearing

Gelling properties of silver carp surimi as affected by different comminution methods: blending and shearing

Effects of high‐speed shear homogenization on the emulsifying and structural properties of myofibrillar protein under low‐fat conditions

Structure and functionalities changes in high-pressure homogenized clam protein isolate

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