Effect of ultrasound on structure and functional properties of laccase-catalyzed α-lactalbumin

Yuan, Xiangying; Li, Xueyan; Zhang, Xinliu; Mu, Zhishen; Gao, Zengli; Jiang, Lianzhou; Jiang, Zhanmei

doi:10.1016/j.jfoodeng.2017.12.008

Cited by 26 publications

(21 citation statements)

References 35 publications

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“…Lac-US-α-lactalbumin and US-α-lactalbumin produced a substantial rise (p < 0.05) in surface hydrophobicity with US time from 0 to 60 min. This outcome was in agreement with Yuan et al [25] stated that surface hydrophobicity of laccase-catalyzed α-lactalbumin in the presence of ferulic acid showed a remarkable increase in comparison with α-lactalbumin and α-lactalbumin incubated with laccase. Furthermore, it was also reported that surface hydrophobicity of WPI increased with an increase of ultrasound power (0–600 W) and pH value (3–11) [65] .…”

Section: Resultssupporting

confidence: 92%

“…Compared with US-α-lactalbumin emulsion, Lac-US-α-lactalbumin emulsion had the formation of polymers around at 120 kDa. Furthermore, Yuan et al [25] stated that there was production of polymers, trimers and dimers of 40–120 kDa in α-lactalbumin treated with laccase and FA. However, with US time prolonged, molecular weight distribution of Lac-US-α-lactalbumin and US-α-lactalbumin emulsion was not changed.…”

Section: Resultsmentioning

confidence: 99%

“…The measured temperature of the Lac-US-α-lactalbumin and US-α-lactalbumin emulsion was below 40 °C. The ultrasound and laccase cross-linking conditions were selected according to the related recent research work [24] , [25] , [26] .…”

Section: Methodsmentioning

confidence: 99%

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Laccase cross-linking of sonicated α-Lactalbumin improves physical and oxidative stability of CLA oil in water emulsion

Qayum

Shi

et al. 2021

Ultrasonics Sonochemistry

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Section: Resultssupporting

confidence: 92%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Laccase cross-linking of sonicated α-Lactalbumin improves physical and oxidative stability of CLA oil in water emulsion

Qayum

Shi

et al. 2021

Ultrasonics Sonochemistry

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“…On these SDS-PAGE, the presence of unique high Molecular-Weight (MW) band is the frequent indication of crosslinked protein formation. In addition, Size Exclusion Chromatography (SEC) was applied to detect for the formation of phytochemical-mediated, protein crosslinking conjugates [31,34,35]. Here, the higher MW protein crosslinking conjugates will be excluded from the pores of the porous beads, and hence eluted in a shorter time from the column.…”

Section: Analytical Methods Used To Study Protein Crosslinking Conjugmentioning

confidence: 99%

“…On the other hand, combination of advanced analytical methods such as Mass Spectrometry (MS) [25,27,29,36], high performance liquid chromatography [26,29], and fluorescence spectroscopy [33,34,35] were also reportedly applied to investigate the laccase-catalyzed, phytochemical-mediated protein crosslinking. For instance, in a tandem MS study, the finding helped to provide supporting evidence as to the functional roles of tyrosine and cysteine residues in the crosslinked mechanism [36].…”

Section: Analytical Methods Used To Study Protein Crosslinking Conjugmentioning

confidence: 99%

Laccase‐catalyzed, Phytochemical‐mediated Protein Crosslinking Conjugates

Chai

Xiao

Dass

et al. 2020

eFood

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Laccase is a Class 1 oxidoreductase enzyme, which catalyzes the oxidation of a wide range of phenolic substrates. Previously, several reviews had highlighted on the industrial importance of laccase, including in food industry. Similarly, the ability of laccase to crosslink and polymerize food protein molecules had also been reviewed. However, no much review information is available on the crosslinking of protein molecules, mediated by phytochemicals. In this review, we highlighted on the laccase-catalyzed, phytochemical-mediated protein crosslinking conjugates, and their associated functional changes, reported by different research groups over the last 10 years. In many of these reported studies, milk protein components are utilized, along with the addition of selected phytochemicals (chlorogenic acid, ferulic acid). As proteins are major dietary components, while phytochemicals are plant-derived chemicals with well-studied bioactivities, their conjugations could potentially lead to the identification of novel health-promoting compounds.

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Comparison of interaction, structure, and cell proliferation of α‐lactalbumin–safflower yellow complex induced by microwave heating or conventional heating

Huang

et al. 2022

J Sci Food Agric

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Background The protein–polyphenol interaction mechanism has always been a research hotspot, but their interaction is affected by heat treatment, which is widely applied in food processing. Moreover, the effects of microwave or water‐bath heating on the protein–polyphenol interaction mechanism have been not clarified. The pasteurization condition (65 °C, 30 min) was selected to compare the effects of microwave or water bath on binding behavior, structure, and cell proliferation between α‐lactalbumin (α‐LA) and safflower yellow (SY), thus providing a guide for the selection of functional dairy processing conditions. Results Microwave heat treatment of α‐LA–SY resulted in stronger fluorescence quenching than that of conventional heat treatment. Moreover, the binding constant Ka of all α‐LA–SY samples was augmented significantly after microwave or water bath treatment, and microwave‐heated α‐LA–SY showed the maximum Ka. Fourier transform infrared spectroscopy showed that microwave heating resulted in more ordered structures of α‐LA into its disordered structures than water bath heating. However, the ferric reducing antioxidant power and chroma value of α‐LA–SY were more reduced by microwave heating than by water bath heating. Moreover, microwave heating facilitated the cell proliferation of α‐LA–SY compared with water bath treatment. Conclusion It was demonstrated that microwave heating promoted interaction between α‐LA and SY more than water bath heating did. Microwave heat treatment was a safe and effective way to enhance the binding affinity of α‐LA to SY, being a potential application in food industry. © 2022 Society of Chemical Industry.

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Effect of ultrasound on structure and functional properties of laccase-catalyzed α-lactalbumin

Cited by 26 publications

References 35 publications

Laccase cross-linking of sonicated α-Lactalbumin improves physical and oxidative stability of CLA oil in water emulsion

Laccase cross-linking of sonicated α-Lactalbumin improves physical and oxidative stability of CLA oil in water emulsion

Laccase‐catalyzed, Phytochemical‐mediated Protein Crosslinking Conjugates

Comparison of interaction, structure, and cell proliferation of α‐lactalbumin–safflower yellow complex induced by microwave heating or conventional heating

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