Comparative studies on the interaction of [C4mim]Br, and [C8mim]Br with β-casein micelles

Liu, Yanping; Liu, Yang; Mao, Huiyuan; Guo, Rong

doi:10.1016/j.colsurfa.2013.10.012

Cited by 10 publications

(13 citation statements)

References 49 publications

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“…This can be attributed to the great hydrophobicity of these ILs. In general, when hydrophobic interactions occur, they lead to a decrease in Δ H obs . , Chabba et al, in the titration of three surface-active ionic liquids (SAILs) into a polymer solution of Pluronic F108, showed that the titration of all three SAILs into the polymeric solution resulted in endothermic heat changes when compared to the titration of SAILs into water at 25 °C.…”

Section: Resultsmentioning

confidence: 99%

Heteroassembly Ability of Dicationic Ionic Liquids and Neutral Active Pharmaceutical Ingredients

et al. 2018

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Extensive investigation of interactions and aggregation properties of IL + API systems is necessary to apply ionic liquids (ILs) with different hydrophobic characteristics to drug delivery or in active pharmaceutical ingredient (API) formulations. Therefore, this study aims to investigate the heteroassembly between dicationic ILs ([BisOct(MIM) 2 ][2X], in which X is Br or BF 4 , and [BisOct(BnIM) 2 ][2Br]), both in the absence and the presence of neutral APIs (salicylic acid, ibuprofen, and paracetamol) with different functional groups. Isothermal titration calorimetry results demonstrate that IL–API associations occur at very low concentrations of IL. These results were reinforced by electrospray ionization mass spectrometry with variable collision-induced dissociation, in which the IL dication interactions with APIs were detected. The strength of the dication–API interaction was determined from E cm,1/2 data. The aggregation parameters (cac, Δ G agg ° , and K ) between ILs and APIs were evaluated by conductivity. The 1 H NMR data showed that differences in chemical shifts provided relevant insights about interaction sites in both components.

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Section: Resultsmentioning

confidence: 99%

Heteroassembly Ability of Dicationic Ionic Liquids and Neutral Active Pharmaceutical Ingredients

et al. 2018

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“…31 As reported, α s1 -casein and α s2 -casein each possesses two Trp residues, that is, (Trp-164 and Trp-199) and (Trp-109 and Trp-193), respectively, whereas β-casein contains a single Trp143 residue in the hydrophobic C-terminal region. 14,31 Figure 8 exhibits the fluorescence spectra of casein with different concentrations of BQAS, SGS, RL, SL, and SDS at 298 K. As shown in Figure 8a, BQAS caused a slight decrease in fluorescence spectra of casein, followed by a sharp increase. Specifically, when c BQAS increased to 0.1 mmol/L, C 1 in the turbidity titration curve and fluorescence intensity of casein reached the minimum.…”

Section: ζ-Potentialmentioning

confidence: 98%

“…13 On the other hand, Guo et al studied the interaction of ionic-liquid-type surfactants with β-casein micelles. 14 In bulk solutions, the influences of surfactants on interfacial adsorption of protein molecules and properties of interfacial films have been extensively examined. For nonionic surfactants, Miller et al studied the effects of nonionic surfactants on the adsorption of casein molecules.…”

Section: Introductionmentioning

confidence: 99%

“…Furthermore, dodecyl ammonium chloride, as a cationic surfactant, interacts with sodium caseinate through hydrophobic and hydrophilic groups, inducing the structural transition of self-aggregates, which are determined primarily by surfactant aggregation states, such as monomeric and micellar states . On the other hand, Guo et al studied the interaction of ionic-liquid-type surfactants with β-casein micelles …”

Section: Introductionmentioning

confidence: 99%

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Interaction Mechanism of Different Surfactants with Casein: A Perspective on Bulk and Interfacial Phase Behavior

Tian

Lai

Zhou³

et al. 2019

J. Agric. Food Chem.

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Understanding the interaction mechanism between proteins and surfactants is conducive to the application of protein/surfactant mixtures in the food industry. The present study investigated the interaction mechanism of casein with cationic Gemini surfactant (BQAS), anionic Gemini surfactant (SGS), anionic single-chain surfactant (sodium dodecyl sulfate [SDS]), and two biosurfactants (rhamnolipid [RL] and lactone sophorolipid [SL]) at the interface and in bulk phase. BQAS/casein and SDS/casein mixtures exhibit a strong synergistic effect on the surface activity. For SGS, RL, and SL, the formation of surfactant/casein complexes caused no improvement in surface activity. Dilational elasticity results indicate the displacement of casein by SGS, RL, and SL at the surface. However, the BQAS/casein complexes manifested varying dilational properties from pure casein surface. The strong electrostatic interaction between BQAS and casein produced large-size precipitate particles. For other surfactants, no precipitate particles formed. Determination of ζ-potential, UV–vis absorption spectra, and fluorescence spectra demonstrated the stronger interaction of BQAS and SDS with casein than that of SGS, RL, and SL. Addition of BQAS initially increased and then decreased the α-helix structure of casein. For SGS, RL, and SL, no noticeable change occurred in the casein structure. However, the formation of SDS/casein complexes was conducive to the casein structure. In conclusion, the interaction between BQAS and casein is similar to that of cationic single-chain surfactant. Furthermore, SGS exhibits a significantly different interaction mechanism from the corresponding monomer (SDS), possibly resulting from its excellent interfacial activity, low critical micelle concentration values, and strong self-assembly capability. For RL and SL, the weak interaction is attributed to the relatively complicated structure and less charged degree of hydrophilic headgroups.

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“…Polypeptides and proteins from animals can serve as the hydrophilic component of surfactants as inherently foamy and emulsifiers, such as lysozyme (Bhat et al, 2018; Chernysheva et al, 2018; Janek et al, 2017), casein (Liu et al, 2014; Wojciechowski et al, 2014), and whey protein isolate (Cai and Ikeda, 2016; Drapala et al, 2016; Gaspar et al, 2017). Others are rich in collagen, keratin, and elastin.…”

Section: Introductionmentioning

confidence: 99%

Preparation of Polypeptide Surfactants Using Chromium‐Containing Waste Leather: Effect of Hydrophilic and Lipophilic Groups

Sun

Jiang

et al. 2021

J Surfact & Detergents

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Polypeptide surfactants with different lengths of hydrophilic groups and lipophilic groups were synthesized from collagen hydrolysate polypeptides by the Schotten‐Baumann reaction. Collagen hydrolysate polypeptides were prepared through alkaline hydrolysis of chromium‐containing leather wastes, followed by changing the molecular weight of the collagen hydrolysate and the carbon chain length of the acid chloride. Fourier transform infrared spectroscopy, confirmed the successful synthesis of the polypeptide surfactants. Furthermore, surface activities of surfactants were tested to reflect the influence of the length of hydrophilic and lipophilic groups on properties, such as surface tension, foamability, foam stability, wettability, and Hydrophile–Lipophile Balance value. The results indicated that for surfactants prepared from collagen hydrolysate, a shorter hydrophilic group length resulted in lower surface tension and better foamability, foam stability, and a wetting ability which indicates the surfactants can be used as wetting agents. In contrast, the surfactant with a greater lipophilic group length had lower surface tension and poorer foamability, foam stability, and wetting ability. The presence of the C=C bond of the oleoyl lipophilic group decreased surface tension. The polypeptide surfactants prepared from collagen hydrolysate not only can effectively utilize chromium‐containing leather solid waste produced, but also avoid environmental pollution and promote the sustainable development of the leather industry.

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Comparative studies on the interaction of [C4mim]Br, and [C8mim]Br with β-casein micelles

Cited by 10 publications

References 49 publications

Heteroassembly Ability of Dicationic Ionic Liquids and Neutral Active Pharmaceutical Ingredients

Heteroassembly Ability of Dicationic Ionic Liquids and Neutral Active Pharmaceutical Ingredients

Interaction Mechanism of Different Surfactants with Casein: A Perspective on Bulk and Interfacial Phase Behavior

Preparation of Polypeptide Surfactants Using Chromium‐Containing Waste Leather: Effect of Hydrophilic and Lipophilic Groups

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