Thermal unfolding of β‐lactoglobulin, α‐lactalbumin, and bovine serum albumin. A thermodynamic approach

Relkin, Perla; Mulvihill, D.M.

doi:10.1080/10408399609527740

Cited by 166 publications

(127 citation statements)

References 138 publications

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“…Such results agree with those of Paulsson and Dejmek 10 who also observed a decrease in the β-lactoglobulin denaturation temperature in the presence of casein fractions. A decrease in the denaturation temperature of β-lactoglobulin with increasing pH was also reported by Mulvihill and Donovan 18 , Relkin and Mulvihill 19 , and Baeza and Pilosof 9 .…”

Section: Discussionsupporting

confidence: 58%

Heat-Induced Whey Protein Gels: Effects of pH and the Addition of Sodium Caseinate

Picone

Takeuchi²,

Cunha

2010

Food Biophysics

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The effects of pH (6.7 or 5.8), protein concentration and the heat treatment conditions (70 or 90°C) on the physical properties of heat-induced milk protein gels were studied using uniaxial compression, scanning electron microscopy, differential scanning calorimetry, and water-holding capacity measurements. The systems were formed from whey protein isolate (10-15% w/v) with (5% w/v) or without the addition of caseinate. The reduction in pH from 6.7 to 5.8 increased the denaturation temperature of the whey proteins, which directly affected the gel structure and mechanical properties. Due to this increase in the denaturation temperature of the β-lactoglobulin and α-lactalbumin, a heat treatment of 70°C/30 min did not provide sufficient protein unfolding to form self-supporting gels. However, the presence of 5% (w/v) sodium caseinate decreased the whey protein thermo stability and was essential for the formation of self-supporting gels at pH 6.7 with heat treatment at 70°C/30 min. The gels formed at pH 6.7 showed a fine-stranded structure, with great rigidity and deformability as compared to those formed at pH 5.8. The latter had a particulate structure and exuded water, which did not occur with the gels formed at pH 6.7. The addition of sodium caseinate led to less porous networks with increased gel deformability and strength but decreased water exudation. The same tendencies were observed with increasing whey protein concentration.

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Section: Discussionsupporting

confidence: 58%

Heat-Induced Whey Protein Gels: Effects of pH and the Addition of Sodium Caseinate

Picone

Takeuchi²,

Cunha

2010

Food Biophysics

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“…It was supposed in this study that ␣-la and CSA are involved in deposition phenomenon. The differences between camel rennet and acid wheys occured in their chemical compositions, mainly in pH (6.51 and 4.3 for camel rennet and acid wheys, respectively) and mineralization (Relkin, 1996). Indeed, pH has an impact on the thermal behavior of whey proteins, mainly ␣-la, which is the major protein in camel whey.…”

Section: Discussionmentioning

confidence: 99%

A laboratory investigation of cow and camel whey proteins deposition under different heat treatments

Felfoul

Lopez

Gaucheron

et al. 2015

Food and Bioproducts Processing

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“…Cation binding to the strong calcium-binding site increases considerably the stability of the protein under the action of heating and other denaturing agents such as urea and guanidine hypochloride [3]. As demonstrated by differential scanning calorimetric data, the binding of calcium shifts the heat transition to higher temperatures by about 308C [7].…”

mentioning

confidence: 98%

Study of ethanol‐induced conformational changes of holo and apo α‐lactalbumin by spectroscopy and limited proteolysis

Wehbi¹,

Pérez²,

Dalgalarrondo³

et al. 2006

Molecular Nutrition Food Res

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This study was performed to contribute to the analysis of alpha-lactalbumin "molten globule" state by using spectral and proteolysis techniques. Samples of holo and apo alpha-lactalbumin in the presence of different concentrations of ethanol were analyzed. Results of fluorescence spectroscopy of both forms showed that as ethanol concentration increased, the tryptophanyl residues became more accessible to the solvent. Near circular dichroism spectra of holo alpha-lactalbumin indicated that its tertiary structure was maintained in 20% ethanol whereas it was altered in 30 and 40% ethanol. For apo alpha-lactalbumin, spectra were similar in all samples studied. Holo alpha-lactalbumin was resistant to trypsinolysis in 0% ethanol, whereas it was easily hydrolyzed in 20 and 30% ethanol. In the case of the apo form and in the absence of ethanol, 70% of the protein was degraded after 1 h. However, in the presence of 20 and 30% ethanol, the overall reaction rate was lowered. Peptides obtained after tryptic hydrolysis were identified by reversed-phase high-performance liquid chromatography coupled to mass spectrometry. Differences in population of produced peptides indicate the changes of folding intermediates present in the studied alpha-lactalbumin solutions. This study demonstrated that proteolytic enzymes are suitable tools to determine protein structure complementing physico-chemical studies.

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Thermal unfolding of β‐lactoglobulin, α‐lactalbumin, and bovine serum albumin. A thermodynamic approach

Cited by 166 publications

References 138 publications

Heat-Induced Whey Protein Gels: Effects of pH and the Addition of Sodium Caseinate

Heat-Induced Whey Protein Gels: Effects of pH and the Addition of Sodium Caseinate

A laboratory investigation of cow and camel whey proteins deposition under different heat treatments

Study of ethanol‐induced conformational changes of holo and apo α‐lactalbumin by spectroscopy and limited proteolysis

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