2019
DOI: 10.1016/j.ijbiomac.2019.03.076
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Interfacial and enhanced emulsifying behavior of phosphorylated ovalbumin

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Cited by 58 publications
(25 citation statements)
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“…argued that all possible vulnerable phosphate sites from ovalbumin were merely located on serine 221, 269, and 281 residues and tyrosine 281 under wet‐heating conditions (Sheng et al., 2019). They further pointed out phosphorylation rendered ovalbumin molecular to become more flexible and disordered, which is consistent with the research conducted by other researchers (Sheng et al., 2019; Tang et al., 2019). Considering protein functionalities, such as solubility, thermal stability, apparent viscosity, emulsification, and foaming properties, the hydrophilic phosphorylation of a protein resulted in a distinct enhancement in such intriguing properties (Hao et al., 2019; Sheng et al., 2019; Tang et al., 2019; Wang et al., 2019; Xiong et al., 2016; Yang et al., 2019).…”
Section: Chemical Modificationsupporting
confidence: 87%
“…argued that all possible vulnerable phosphate sites from ovalbumin were merely located on serine 221, 269, and 281 residues and tyrosine 281 under wet‐heating conditions (Sheng et al., 2019). They further pointed out phosphorylation rendered ovalbumin molecular to become more flexible and disordered, which is consistent with the research conducted by other researchers (Sheng et al., 2019; Tang et al., 2019). Considering protein functionalities, such as solubility, thermal stability, apparent viscosity, emulsification, and foaming properties, the hydrophilic phosphorylation of a protein resulted in a distinct enhancement in such intriguing properties (Hao et al., 2019; Sheng et al., 2019; Tang et al., 2019; Wang et al., 2019; Xiong et al., 2016; Yang et al., 2019).…”
Section: Chemical Modificationsupporting
confidence: 87%
“…Five mL of solution was filtered through a membrane filter (diameter, 13 mm; pore size, 0.45 μm) (Sartorius, Gottingen, Germany) and diluted twice with PBS buffer (0.01 g/L, pH 7.4). The Nano-ZS90 (Malvern Instruments Ltd., UK) by placing the sample (0.75 mL) in the high concentration cell equipped with a transparent electrode was used to determine the zeta potential of ME white samples [11] .…”
Section: Methodsmentioning
confidence: 99%
“…As the main protein in egg white, OVA contained more than half of hydrophobic amino acids mostly buried inside the molecule, resulting in the low surface hydrophobicity and limiting EWP applications (Wang et al., 2019). Many methods were used to improve emulsifying property of EWP, such as acid treatment, acid‐heat treatment, ultrasonic treatment, and protein modification technology (Ai et al., 2020; Chang et al., 2016; Stefanović et al., 2017; Tang et al., 2019). However, some chemical treatment had a potential risk and was difficult to be applied widely into food industries.…”
Section: Functional Properties Of Ewpmentioning
confidence: 99%