The activity and molecular interaction of lysozyme in adding four ionic liquids aqueous solutions

Li, Na; Wang, Ying; Dang, Leping; Zhang, Bo; Wang, Zhanzhong

doi:10.1016/j.molliq.2022.118788

Cited by 7 publications

(2 citation statements)

References 34 publications

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“…As reported in the literature, the natural conformation of Lys molecules consisted mainly of six Tryptophan (Trp) residues containing hydrophobic microregions. Owing to the damage to the tertiary structure of Tryptophan, the hydrophobic groups such as Trp would be exposed to the polar environment and provide the primary driving force for the gathering process [15,16]. As can be seen from Figure 5, the fluorescence of Trp in the bulk phase after the addition of reduced GSH expanded at 380 nm as against natural Lys.…”

Section: Reduction Of Disulfide Bonds In Defolded Lysmentioning

confidence: 99%

Mechanism of Reduced Glutathione Induced Lysozyme Defolding and Molecular Self-Assembly

Guo

Hou

Liang

et al. 2023

Foods

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The distinctive assembly behaviors of lysozyme (Lys) feature prominently in food, materials, biomedicine, and other fields and have intrigued many scholars. Although our previous work suggested that reduced glutathione (GSH) could induce lysozyme to form interfacial films at the air/water interface, the underlying mechanism is still obscure. In the present study, the effects of GSH on the disulfide bond and protein conformation of lysozyme were investigated by fluorescence spectroscopy, circular dichroism spectroscopy, and infrared spectroscopy. The findings demonstrated that GSH was able to break the disulfide bond in lysozyme molecules through the sulfhydryl/disulfide bond exchange reaction, thereby unraveling the lysozyme. The β-sheet structure of lysozyme expanded significantly, while the contents of α-helix and β-turn decreased. Furthermore, the interfacial tension and morphology analysis supported that the unfolded lysozyme tended to arrange macroscopic interfacial films at the air/water interface. It was found that pH and GSH concentrations had an impact on the aforementioned processes, with higher pH or GSH levels having a positive effect. This paper on the exploration of the mechanism of GSH-induced lysozyme interface assembly and the development of lysozyme-based green coatings has better instructive significance.

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Section: Reduction Of Disulfide Bonds In Defolded Lysmentioning

confidence: 99%

Mechanism of Reduced Glutathione Induced Lysozyme Defolding and Molecular Self-Assembly

Guo

Hou

Liang

et al. 2023

Foods

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“…Lysozyme (LYS), also known as muramidase, is a protein found in microorganisms, plants, and animals. − LYS has been widely used in the food industry for its excellent biocompatibility, outstanding bactericidal, and easy accessibility. − Owing to its exposed internal hydrophobic amino acids, the conformation of LYS can be easily altered by solvent or pH conditions. For example, when the pH is lower than its isoelectric point (10.5), LYS is positively charged and can interact with negatively charged polysaccharide molecules to form micro- or nanoscale LYS–polysaccharide carriers, mainly through electrostatic forces .…”

Section: Introductionmentioning

confidence: 99%

pH-Driven Self-Assembly of Functional Lysozyme–Hyaluronan Complex Colloidal Nanoparticles for the Oral Delivery of Lutein

Liu,

Li,

Lian

et al. 2024

Crystal Growth & Design

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Despite its various health-promoting bioactivities, poor water solubility, chemical instability, and low bioavailability of lutein have limited its further application in the food industry. This paper reports a simple and a green pH-driven method to synthesize lutein-loaded lysozyme−hyaluronan complex colloidal nanoparticles (Lut@LYS-HANPs) able to overcome the aforementioned shortcomings. The fabricated Lut@LYS-HANPs exhibited a stabilized particle size (164 nm), negative surface zetapotential (−44.86 mV), excellent long-term storage stability, and favorable redispersibility. The encapsulation efficiency and loading ability of lutein in the prepared Lut@LYS-HANPs were 96.23 and 11.07%, respectively. Infrared spectra demonstrated that the dominant interaction forces behind the formed Lut@LYS-HANPs were hydrogen bonds and hydrophobic and electrostatic interactions. The circular dichroism spectra indicated that lutein incorporation mainly changed the α-helix and β-sheet contents of lysozyme. Besides, the

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Efficient combination of ionic-liquid-based ultrasound-assisted extraction, complex chromatography, and molecular docking for screening of acetylcholinesterase inhibitors from Ganoderma atrum

Hou

Liu

et al. 2022

Food Measure

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The activity and molecular interaction of lysozyme in adding four ionic liquids aqueous solutions

Cited by 7 publications

References 34 publications

Mechanism of Reduced Glutathione Induced Lysozyme Defolding and Molecular Self-Assembly

Mechanism of Reduced Glutathione Induced Lysozyme Defolding and Molecular Self-Assembly

pH-Driven Self-Assembly of Functional Lysozyme–Hyaluronan Complex Colloidal Nanoparticles for the Oral Delivery of Lutein

Efficient combination of ionic-liquid-based ultrasound-assisted extraction, complex chromatography, and molecular docking for screening of acetylcholinesterase inhibitors from Ganoderma atrum

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