Effect of disulfide bond cleavage on structural and interfacial properties of whey proteins

Kella, Navin Kumar D.; Yang, Syng T.; Kinsella, John E.

doi:10.1021/jf00089a001

Cited by 57 publications

(50 citation statements)

References 19 publications

(40 reference statements)

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“…If a substantial number of disulfide groups were cleaved by Na 2 SO 3 to generate thiosulfonate derivatives, the T d of the Na 2 SO 3 -steeped beans should be lower than the Na 2 S 2 O 5 -steeped beans. On the other hand, Kella et al (20) reported that thiosulfonate derivatives of whey proteins, generated by action of Na 2 SO 3 , brought about structural changes that exposed nonpolar groups buried inside the protein interior. This finding would cause a heat-stabilizing rather than heat-destabilizing effect.…”

Section: Resultsmentioning

confidence: 99%

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Effect of salts on soy storage proteins defatted with supercritical CO₂ and alcohols

Sessa

Nelsen

Snyder

1998

J Americ Oil Chem Soc

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The primary objective was to determine whether salts will stabilize soy storage proteins against the denaturing effects of alcohols or the heat and pressure used in supercritical CO 2 during the defatting process. Nitrogen solubility index (NSI) and differential scanning calorimetry (DSC) were used to monitor the denaturation of proteins. A variety of salt solutions used to hydrate full-fat soy grits increased the thermal stability of both 7S and 11S storage proteins. DSC was used to monitor their denaturation temperature. Neutral salt hydrations followed the lyotropic series for protein stabilization. Of the salts evaluated, the test results indicate that the reducing salt, sodium sulfite, and the neutral salt, sodium sulfate, when used to steep beans, yielded significantly higher NSI than did the watersteeped controls or other salt treatments after partial defatting with absolute isopropanol or ethanol and supercritical CO 2 . However, these same salt treatments did not as effectively stabilize the proteins against the denaturing effects of ethanol more aqueous than 84% when these alcohols were used as the defatting medium. JAOCS 75, 911-916 (1998).KEY WORDS: Defatting, differential scanning calorimetry, ethanol extraction of oil, heat denaturation, isopropanol extraction of oil, nitrogen solubility index, salt stabilization, soybeans, supercritical CO 2 extraction of oil.For the development of new methodologies to process soy with desired functional properties, the researcher must control the protein denaturation process. It is generally recognized that a high level of solubility reflects a versatile protein with good potential for use in either food or industrial product systems. Denaturing conditions, such as exposure to heat, high pressure, high shear, or organic solvents, tend to lower protein solubility. The denaturation process for soy storage proteins in the heterogeneous cracked bean system is extremely complex, particularly at low to intermediate moisture. Fats, carbohydrates, and nonprotein constituents not only impact the moisture dynamics in the whole bean but also impact the expected protein-solvent and protein-protein interactions during denaturation. Salt stabilization of proteins in solution is an old technology that has already been well researched. However, limited information is available on salt stabilization to protect protein from denaturation during processing under limited-moisture conditions. At high salt concentration (µ > 0.5), the ability of salts to stabilize proteins has been attributed to preferential hydration of the protein molecule as a result of the salt-induced alteration of the water structure in the vicinity of the protein (1). At high concentrations of neutral salts, proteins display decreased solubility, which may result in precipitation due to a salting-out phenomenon. Salting-out reduces solute-solvent contact and enhances solute-solute contact or entanglement by making water a poor solvent for the protein.Here, protein-protein interactions are favored over protein-sol...

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Section: Resultsmentioning

confidence: 99%

“…Protein solubility results from the balance of the attraction of protein molecules for each other and the solvent molecules for the solute (27). The reducing salt Na 2 SO 3 will cleave disulfide bonds with introduction of a negatively charged sulfonate group: PS-SP + SO 3 2− ⇒ PS-SO 3 − + PS − where P = protein (20).…”

Section: Resultsmentioning

confidence: 99%

Effect of salts on soy storage proteins defatted with supercritical CO₂ and alcohols

Sessa

Nelsen

Snyder

1998

J Americ Oil Chem Soc

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“…Genetically or chemically modified β-LG with added free thiol groups may be a good means to increase branching of the heat-induced whey protein/κ-casein complexes, but this is yet to be demonstrated. Reduction or disruption of natural disulphide bonds (Bazinet et al 1997;Kella et al 1989) may also open routes for branching. Although goat or sheep κ-caseins contain three cysteines, they all seem to be naturally involved into disulphide bonds (Bouguyon et al 2006) and hence, are unlikely to promote branching.…”

Section: Possible Methods To Modify the Size Of The Heat-induced Wheymentioning

confidence: 99%

“…Reduction of part of the disulphide bonds can be performed using chemical agents like β-mercaptoethanol (Goddard 1996;Surel and Famelart 2003) or food-grade alternatives (Kella et al 1989). By applying electroreduction on whey protein ingredients, Bazinet et al (1997) could modulate thiol/disulphide-mediated aggregation and reported correlated changes in thermal gelation behaviour.…”

Section: Structure and Mechanical Properties Of Acid Dairy Gelsmentioning

confidence: 99%

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How to tailor heat-induced whey protein/κ-casein complexes as a means to investigate the acid gelation of milk—a review

Morand

Guyomarc’H

Famelart

2011

Dairy Science & Technol.

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The heat treatment of milk greatly improves the acid gelation of milk and is therefore largely applied in yoghurt manufacture. During the heat treatment, soluble and micelle-bound whey protein/κ-casein complexes are produced in milk. The complexes and their physico-chemical properties have been held responsible for the early gelation point, the increased final firmness and for the serum retention capacity of the acid gels made of heated milk. They are suspected to bring new functionalities to the casein micelles and to help the formation of interactions when building the gel network. In order to investigate the type of interactions that the complexes can affect throughout the acid gelation of milk, an original strategy would be to control the physico-chemical properties of the whey protein/κ-casein soluble complexes and to use them as vectors to modify the possible interactions in the milk. In that perspective, the different physico-chemical properties of the whey protein/κ-casein soluble complexes that are thought to significantly affect the acid gelation behaviour of the casein micelles are listed. Then, the physical, chemical and biological means that could possibly be applied to the formation of complexes in order to modulate each of the targeted property are reviewed and evaluated. In order to open a large choice for future investigation, these methods were found in a larger literature resource than milk, including other protein systems like model whey protein solutions or non-dairy globular protein systems. The food-compatible

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Laser‐induced volume changes during confocal Raman microscopy of whey‐protein‐stabilized emulsions and their relationship to protein content and particle diameters

Iljina

Euston

Bookey

2013

J Raman Spectroscopy

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The use of confocal Raman microscopy is applied to the study of whey‐protein‐stabilized oil‐in‐water emulsions. The stability of emulsions is an important parameter for many applications and is dependent on several factors including protein content and particle size. Emulsions were prepared with varying particle size ranging from 0.8 to 10.0 µm. Changes in sample volume due to laser‐induced heating were monitored and correlated to protein content in samples and to particle diameters. It was found that samples with the lowest protein content and larger particle diameters experienced the largest volume changes. The newly developed approach is of a potential predictive use. Copyright © 2013 John Wiley & Sons, Ltd.

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Effect of disulfide bond cleavage on structural and interfacial properties of whey proteins

Cited by 57 publications

References 19 publications

Effect of salts on soy storage proteins defatted with supercritical CO₂ and alcohols

Effect of salts on soy storage proteins defatted with supercritical CO₂ and alcohols

How to tailor heat-induced whey protein/κ-casein complexes as a means to investigate the acid gelation of milk—a review

Laser‐induced volume changes during confocal Raman microscopy of whey‐protein‐stabilized emulsions and their relationship to protein content and particle diameters

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Effect of disulfide bond cleavage on structural and interfacial properties of whey proteins

Cited by 57 publications

References 19 publications

Effect of salts on soy storage proteins defatted with supercritical CO2 and alcohols

Effect of salts on soy storage proteins defatted with supercritical CO2 and alcohols

How to tailor heat-induced whey protein/κ-casein complexes as a means to investigate the acid gelation of milk—a review

Laser‐induced volume changes during confocal Raman microscopy of whey‐protein‐stabilized emulsions and their relationship to protein content and particle diameters

Contact Info

Product

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Effect of salts on soy storage proteins defatted with supercritical CO₂ and alcohols

Effect of salts on soy storage proteins defatted with supercritical CO₂ and alcohols