Use of l-arginine-assisted ultrasonic treatment to change the molecular and interfacial characteristics of fish myosin and enhance the physical stability of the emulsion

Shi, Ting; Liu, Hui; Song, Teng; Xiong, Zhiyu; Li, Yuan; McClements, David Julian; Jin, Wengang; Sun, Quancai; Gao, Ruichang

doi:10.1016/j.foodchem.2020.128314

Cited by 37 publications

(12 citation statements)

References 36 publications

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“…Followed by ZCPs and ZKCPs, 35.17 ± 1.53 and 30.26 ± 1.07%, respectively, indicating that the addition of Lys could increase the amount of adsorbed proteins. Notably, the change of adsorbed protein was consistent with that of particle size, which was also confirmed in the study by Shi et al ( 39 ). The separation of colloidal particles from the interface needs to break through a vast reverse desorption energy barrier, which makes the adsorption irreversible and endows Pickering emulsion with high stability ( 40 ).…”

Section: Resultssupporting

confidence: 88%

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Improvement of Storage Stability of Zein-Based Pickering Emulsions by the Combination of Konjac Glucomannan and L-Lysine

et al. 2022

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In this work, L-lysine (Lys) was employed together with konjac glucomannan (KGM) to fabricate zein colloidal particles (ZCPs) aimed at enhancing the storage stability of Pickering emulsions. With the addition of Lys, zein-Lys colloidal particles (ZLCPs) and zein-Lys-KGM (ZLKCPs) exhibited smaller particle size (133.64 ± 1.43, 162.54 ± 3.51 nm), polydispersity index (PDI) (0.10 ± 0.029, 0.13 ± 0.022), π value, and more adsorbed protein. Meanwhile, KGM underwent deamidation in an alkaline solution, so the emulsions stabilized by ZLKCPs exhibited a solid gel-like structure with higher storage modulus (G′) and loss modulus (G′′), leading to lower fluidity and better stability. The synergistic effects of Lys and KGM improved the stability of the emulsion. Hydrophobic interactions and hydrogen bonds were the main driving forces forming colloidal particles, which were determined by driving force analysis.

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Section: Resultssupporting

confidence: 88%

“…As an emulsifier, colloidal particles adsorb on the surface of the oil drop, leaving the hydrophilic sides in contact within the aqueous phase ( 39 ). As shown in Figure 6A , ZLCPs and ZLKCPs exhibited the highest surface-adsorbed proteins, 52.02 ± 2.02 and 51.83 ± 1.86%, respectively.…”

Section: Resultsmentioning

confidence: 99%

Improvement of Storage Stability of Zein-Based Pickering Emulsions by the Combination of Konjac Glucomannan and L-Lysine

et al. 2022

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“…Previous work has reviewed that High intensity ultrasound (HIU) treatment is applicable in producing highly stabilized protein emulsions ( 67 ). The pretreatment of protein with HIU also potentially affects its emulsion abilities as determined by HIU mode, treatment period, ultrasound frequency, and intensity ( 68 – 70 ). Since the sonication might lead to highly exposed hydrophobic groups in proteins, it could effectively increase oil adsorption capacity and emulsion stability ( 69 ).…”

Section: Emulsion Related Characteristics Of Proteinmentioning

confidence: 99%

“…Since the sonication might lead to highly exposed hydrophobic groups in proteins, it could effectively increase oil adsorption capacity and emulsion stability ( 69 ). It should be emphasized that HIU is often synergistically utilized with other treatments in improving emulsion properties of protein, such as HPH ( 63 ), amino acid fortification ( 70 ), and acid treatment ( 71 ). To be specific, combing HPH with HIU improved the interfacial properties of whey protein (improved by 13.97%), among which the former could solely increase the EAI by 8.54% (120 MPa) and the latter could solely enhance the EAI by 7.63% (600 W) ( 72 ).…”

Section: Emulsion Related Characteristics Of Proteinmentioning

confidence: 99%

“…Similar to HPH, HIU-acid treatment improved the emulsifying properties of the soy protein isolate by dissociating aggregates, unfolding structure, and forming soluble aggregate ( 71 ). Also, through facilitating hydrophobic groups exposure and promoting more ordered structure formation, HIU-Arg addition contributed to myosin with better interfacial activity ( 70 ).…”

Section: Emulsion Related Characteristics Of Proteinmentioning

confidence: 99%

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Thoroughly review the recent progresses in improving O/W interfacial properties of proteins through various strategies

Zhang

Zhang²,

Chen³

et al. 2022

Front. Nutr.

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Along with the future food market developing world widely, the personalized nutrition and rational function food design are found to be urgently attracted. Oil in a water (O/W) emulsion system has an excellent ability to maintain nutraceuticals and thus plays a promising role in producing future functional foods. Understanding the interfacial related mechanisms involved are essential for improving the quality of food products. Protein can effectively reduce interfacial tension and stable immiscible phases. The interfacial properties of proteins directly affect the emulsion qualities, which have gradually become a prospective topic. This review will first briefly discuss the interfacial-related fundamental factors of proteins. Next, the paper thoroughly overviewed current physical and chemical strategies tailored to improving the interfacial and emulsion properties of proteins. To be summarized, a higher flexibility could allow protein to be more easily unfolded and adsorbed onto the interface but could also possibly form a softer interfacial film. Several physical strategies, such as thermal, ultrasound and especially high-pressure homogenization are well applied to improve the interfacial properties. The interfacial behavior is also altered by various green chemical strategies, such as pH adjustment, covalent modification, and low molecular weight (LMW) surfactant addition. These strategies upgraded emulsion properties by increasing adsorption load, accelerating diffusion and adsorption rate, associated with lowering interfacial tension, and promoting interfacial protein interactions. Future researches targeted at elucidating interfacial-bulk protein interactions, unraveling interfacial behavior through in silico tools, exploring connection between interfacial-industrial processing properties, and clarifying the interfacial-sensory-digestive relationships of O/W emulsions is needed to develop emulsion applications.

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Fat analogue emulsions stabilized by peanut protein microgel particles: microscale and nanoscale structure and stabilization process analysis

Du,

Li,

Meng

2024

J Sci Food Agric

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BACKGROUNDBiopolymer‐based microgels are being regarded increasingly as promising building blocks in food applications. This study aimed to clarify the evolution process of the network for fat analogue emulsions stabilized by peanut protein isolate (PPI) microgel particles. It also investigated the interfacial structure and characteristics of emulsions (50% oil phase, w/w) stabilized by microgels under different pH conditions.RESULTSThere was an increasing interfacial adsorption capacity for PPI microgels over time (from 85.26% to the maximum of 89.78% at 24 h of storage) due to the aggregation of microgels around droplets and the development of cross‐linking microgel chains between adjacent interfaces. The increased β‐sheet content (from 35.51% to 41.12%) of adsorbed microgels indicated unfolding and the enhanced aggregation of microgels, which led to stronger droplet interaction. The network evolution observed with different microscopes clarified the transition to a self‐supporting emulsion. The uneven adsorption of large microgel aggregates at the oil–water interface promoted larger and deformed droplets, so more fat‐like medium internal phase emulsion stabilized by PPI microgel could be obtained by adjusting the microgel pH to 4.5. The interfacial membranes observed by scanning electron microscopy were thicker and coarser at pH 3.0 and 4.5 than those at pH 7.0 and 9.0. The adsorption of PPI microgel aggregates enhanced the structural strength and improved emulsion stability.CONCLUSIONThis work could form a basis for further studies relating physical properties to the design of plant protein‐based fat analogues. © 2024 Society of Chemical Industry.

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Use of l-arginine-assisted ultrasonic treatment to change the molecular and interfacial characteristics of fish myosin and enhance the physical stability of the emulsion

Cited by 37 publications

References 36 publications

Improvement of Storage Stability of Zein-Based Pickering Emulsions by the Combination of Konjac Glucomannan and L-Lysine

Improvement of Storage Stability of Zein-Based Pickering Emulsions by the Combination of Konjac Glucomannan and L-Lysine

Thoroughly review the recent progresses in improving O/W interfacial properties of proteins through various strategies

Fat analogue emulsions stabilized by peanut protein microgel particles: microscale and nanoscale structure and stabilization process analysis

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