Protection effect of sodium alginate against heat-induced structural changes of lactoferrin molecules at neutral pH

Li, Quanyang; Lan, Haijing; Zhao, Zhengtao

doi:10.1016/j.lwt.2018.10.019

Cited by 29 publications

(7 citation statements)

References 27 publications

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“…Bovine serum albumin has a similar isoelectric point to EGF, and its release from a comparable hydrogel network at a pH of 7.4 was strongly dependent on alginate concentration [12]. Additionally, electrostatic behavior within alginate is not influenced by heat treatment [22]. In Figure 8b, it can be clearly seen that the critical temperature is increased with higher netpolymer and alginate concentrations.…”

Section: Thermoresponsivitymentioning

confidence: 93%

“…The pH-dependent, anionic nature of alginate makes a good delivery system for cationic drugs through electrostatic interactions [21]. Sodium alginate interacted with lactoferrin through electrostatic attraction and increased the heat stability of the protein [22]. It is important to consider the lactoferrin isoelectric point of 8.8, giving it a net positive charge in the neutral alginate gel, whereas EGF has an acidic isoelectric point.…”

Section: Thermoresponsivitymentioning

confidence: 99%

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Rheological Investigation of Thermoresponsive Alginate-Methylcellulose Gels for Epidermal Growth Factor Formulation

2020

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Epidermal growth factors (EGF) serve as promising candidates for skin regeneration and rejuvenation products, but their instability hinders them from widespread use. Protective immobilization and directed release can be achieved through implementing a hydrogel delivery system. Alginate and methylcellulose are both natural polymers offering biocompatibility and environmental sensitivity. This blended gel system was investigated rheologically to understand its performance in topical applications. Alginate and methylcellulose were found to form a synergistic gel system that resulted in superior viscosity and thermoresponsiveness compared to the individual components. Increasing methylcellulose concentration directly enhanced gel elasticity, and higher viscosities provided better thermal protection of EGF. The addition of EGF at 3.33 mg/mL resulted in a decrease of viscosity but an increase in viscoelastic modulus. EGF concentration also played a large role in shear viscosity and thermoresponsiveness of the ternary system. An alginate-methylcellulose system presents promising rheological tunability, which may provide EGF thermal protection in a topical delivery format.

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Section: Thermoresponsivitymentioning

confidence: 93%

Section: Thermoresponsivitymentioning

confidence: 99%

Rheological Investigation of Thermoresponsive Alginate-Methylcellulose Gels for Epidermal Growth Factor Formulation

2020

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“…Heat treatment is extensively applied for the processing of such products to inactivate foodborne pathogen and food spoilage bacteria, which may induce denaturation and aggregation of lactoferrin, leading to a decrease or loss of its bacteriostatic activity. Lactoferrin is a heat labile protein, of which the denaturation and aggregation are affected by multiple factors, including iron saturation (Bokkhim, Bansal, GrØndahl, & Bhandari, 2013), pH (Abe et al, 1991;Sreedhara et al, 2010), ionic strength of the solution (Bokkhim et al, 2013;Kawakami, Tanaka, Tatsumi, & Dosako, 1992) or the presence of polysaccharides (Li, Lan, & Zhao, 2019;Xu, Zhao, Guo, & Du, 2019). The protein composition could modify the denaturation kinetics of whey protein.…”

Section: Introductionmentioning

confidence: 99%

Effect of milk serum proteins on aggregation, bacteriostatic activity and digestion of lactoferrin after heat treatment

et al. 2021

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To establish the effect of the presence of milk serum proteins on heat-induced changes to lactoferrin, lactoferrin alone, and lactoferrin mixed with either milk serum or β-lactoglobulin was heated at 65 °C, 70 °C and 75 °C for 30 min. After heating, the effect of milk serum proteins on aggregation of lactoferrin was characterized, after which the effect of such aggregation on digestion and bacteriostatic capacity of lactoferrin were determined. The presence of milk serum proteins accelerated the aggregation of lactoferrin during heating through thiol/disulphide interchange. Lactoferrin also formed disulphide-linked aggregates when it was heated with β-lactoglobulin. Protein aggregates formed at 75 °C were much more resistant to infant digestion, causing decreased peptide release from lactoferrin. Heating lactoferrin and milk serum proteins together accelerated the loss of bacteriostatic activity upon heating. In conclusion, heat-induced aggregation of lactoferrin with milk serum proteins affected both its digestion and its bacteriostatic activity.

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“…It has been extensively applied in the fields of medical, health, biology, food, etc. (Lin et al, 2005;Pawar and Edgar, 2012;Hu et al, 2017;Su et al, 2017;Li et al, 2019). The molecular structure of SA is shown in Figure 1.…”

Section: Introductionmentioning

confidence: 99%

Effects of Sodium Alginate on the Flotation Separation of Molybdenite From Chalcopyrite Using Kerosene as Collector

Zeng

Zhang

et al. 2020

Front. Chem.

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In this paper, the effect of sodium alginate (SA) on the flotation separation of molybdenite (MoS 2) from chalcopyrite using kerosene as collector was systematically investigated. The results of single-mineral micro-flotation tests indicated that SA exhibited strong depression on chalcopyrite flotation while it imposed no impact on the floatability of molybdenite. However, in the chalcopyrite-molybdenite mixed-mineral flotation system, the presence of chalcopyrite significantly increased the depressing effect of SA on molybdenite flotation, leading to a considerable reduction in the flotation selectivity. The negative impact of chalcopyrite on the performance of SA in molybdenite flotation was eliminated by adding a certain dosage of kerosene prior to SA. A concentrate containing 53.43% of molybdenum (Mo) was obtained at 76.90% of recovery using 19 mg/L kerosene and 40 mg/L SA at pH 5.4. Zeta potential measurements indicated that the adsorption of SA on chalcopyrite surfaces was stronger than that on molybdenite surfaces, which agreed with the single-mineral flotation test results. The adsorption of SA on chalcopyrite was further confirmed to be chemisorption by Fourier-transform infrared spectroscopy (FTIR) spectra analyses. When Cu 2+ appeared in solution, the flotation of molybdenite was strongly depressed by SA. Mechanism analyses indicated that more active sites were generated on molybdenite surfaces after the addition of Cu 2+ , thus promoting the adsorption of SA.

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Protection effect of sodium alginate against heat-induced structural changes of lactoferrin molecules at neutral pH

Cited by 29 publications

References 27 publications

Rheological Investigation of Thermoresponsive Alginate-Methylcellulose Gels for Epidermal Growth Factor Formulation

Rheological Investigation of Thermoresponsive Alginate-Methylcellulose Gels for Epidermal Growth Factor Formulation

Effect of milk serum proteins on aggregation, bacteriostatic activity and digestion of lactoferrin after heat treatment

Effects of Sodium Alginate on the Flotation Separation of Molybdenite From Chalcopyrite Using Kerosene as Collector

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