Impact of glycerol on thermostability and heat-induced gelation of bovine serum albumin

Baier, Stefan K.; Decker, Eric A.; McClements, David Julian

doi:10.1016/s0268-005x(03)00046-8

Cited by 49 publications

(51 citation statements)

References 26 publications

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“…For example, the T m value of the b-lg solutions shifted from 75 1C in the absence of cosolvents to 77 1C in the presence of 30 wt% glycerol and 85 1C in the presence of 30 wt% sorbitol. These results are in close agreement with those reported by earlier workers for the influence of glycerol and sorbitol on globular protein thermal stability, e.g., b-lg and BSA (Baier et al, 2004;Baier & McClements, 2003;Chanasattru, Decker, & McClements, 2007a;Dierckx & Huyghebaert, 2002).…”

Section: Influence Of Cosolvents On Protein Conformational Stability supporting

confidence: 93%

“…2). As reported in previous studies, sorbitol was considerably more effective at increasing the thermal stability of the globular protein than glycerol (Baier et al, 2004;Chanasattru, Decker, & McClements, 2007b). Our protein solubility and turbidity measurements indicated that both cosolvents caused a decrease in the free energy of the aggregated state over the non-aggregated state, since there was an increase in the self-association of the globular protein at high cosolvent concentrations (Figs.…”

Section: Article In Presssupporting

confidence: 86%

“…These cosolvents are able to alter the conformation and functional performance of globular proteins in aqueous solutions (McClements, 2002;Saunders, Davis-Searles, Allen, Pielak, & Erie, 2000;Timasheff, 1998Timasheff, , 2002aTimasheff, , 2002b. For example, neutral cosolvents have previously been shown to impact the thermal stability (Baier, Decker, & McClements, 2004;Baier & McClements, 2003;Dierckx & Huyghebaert, 2002), gelation (Baier & McClements, 2001Kulmyrzaev, Bryant & McClements, 2000), foaming (Davis & Foegeding, 2007;Lau & Dickinson, 2005;Murray & Liang, 1999) and emulsion-stabilizing (Kim, Decker & McClements, 2003) performance of globular proteins. The ability of these cosolvents to alter the properties of globular proteins in solution depends on their molecular characteristics, e.g., size, shape and interactions (Timasheff, 1998(Timasheff, , 2002b.…”

Section: Introductionmentioning

confidence: 99%

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Impact of cosolvents (polyols) on globular protein functionality: Ultrasonic velocity, density, surface tension and solubility study

2008

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Section: Influence Of Cosolvents On Protein Conformational Stability supporting

confidence: 93%

Section: Article In Presssupporting

confidence: 86%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Impact of cosolvents (polyols) on globular protein functionality: Ultrasonic velocity, density, surface tension and solubility study

2008

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“…In addition, using sugars (fructose, maltose, sucrose, lactose, glucose, and galactose) and sugar alcohol (sorbitol) also reported to improve heat stability of IgG (Chen & Chang, 1998). Furthermore, Baier et al (2004) observed an improvement on heat stability of BSA at pH 7.0 by glycerol.…”

Section: Influence Of Protectants On Heat Denaturation Of Lf In Liquimentioning

confidence: 92%

“…Depending on glycerol concentration, it can enhances an increase of liquid whey viscosity which in turn reduces the protein-protein interactions (Baier et al 2004). For example, Chanasattru et al (2007) observed that, addition of sorbitol and glycerol raised the denaturation temperature of  -Lg from 74 to 86 o C and 76 o C, respectively.…”

Section: Influence Of Protectants On Heat Denaturation Of Lf In Liquimentioning

confidence: 99%

Heat stability improvement of antimicrobial whey proteins fromyak milk and colostrum at various acidic conditions

Shimo

Ding

et al. 2016

AJDFR

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The aim of this study was to characterize the effect of heat denaturation on Immunoglobulin G (IgG) and Lactoferrin (LF) in yak milk and colostral liquid whey at medium acidic conditions in presence of protectants (CaCl 2 ; Glycerol and Sodium Dodecyl Sulphate -SDS). Results indicated significant (P < 0.05) heat stability improvement of IgG and LF in liquid whey samples at medium acidic and temperature (72 -90 o C) with less precipitates formation regardless of type of protectants added especially at pH 3.5 and 4.6. The mean concentration values for IgG percentage reduction (72 -90 o C; pH 3.5 -5.5; protectants) ranged from 6 to 26% and 15 to 31% in yak milk and colostral liquid whey, respectively. The percentage of heat denaturation effect for LF ranged from 11 to 32% and 14 to 38% in yak milk and colostral liquid whey, respectively. Application of glycerol in both environmental processing conditions was the most effective in heat stability improvement followed by SDS and CaCl 2 .

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Fault‐Tolerant and On‐Demand Supra Tough Adhesive Natural Albumin‐Based Organohydrogels

Chen,

Yang,

Liu

et al. 2024

Adv Funct Materials

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Adhesive hydrogels play a crucial role in numerous applications across fields such as wound dressing, biomedical implants, and flexible electronics. Despite recent efforts on hydrogel design, reconciling the conflicting requirements of adaptability to rough surfaces and intrinsic strength remains elusive for self‐adhesive hydrogels. To address this challenge, a novel strategy is proposed where conformal contact between hydrogels and solids is initially established in a weak state, followed by reinforcement to enhance strength and toughness. Illustrating this approach, bovine serum albumin (BSA) is employed to incorporate a flexible synthetic polymer network, resulting in soft and adhesive organohydrogels (OHGs) with instantaneous and reversible adhesion on various substrates, providing fault‐tolerant operation convenience. A brief on‐demand heating step transforms them into a strong and supra‐adhesive state by forming a rigid BSA network and establishing a double network (DN) structure. The resulting BSA based DN OHGs demonstrate remarkably enhanced bulk mechanical strength and exceptional interfacial toughness on diverse nonporous solid substrates, allowing for on‐demand permanent fixation. This approach integrates fault‐tolerance and permanent fixation into a single material, highlighting the potential of these natural albumin based OHGs as advanced functional materials for diverse applications, including artisanal restoration, and all‐season flexible sensors.

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Impact of glycerol on thermostability and heat-induced gelation of bovine serum albumin

Cited by 49 publications

References 26 publications

Impact of cosolvents (polyols) on globular protein functionality: Ultrasonic velocity, density, surface tension and solubility study

Impact of cosolvents (polyols) on globular protein functionality: Ultrasonic velocity, density, surface tension and solubility study

Heat stability improvement of antimicrobial whey proteins fromyak milk and colostrum at various acidic conditions

Fault‐Tolerant and On‐Demand Supra Tough Adhesive Natural Albumin‐Based Organohydrogels

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