Specific Disulfide Bond in α‐Lactalbumin Infiuences Heat‐ Induced Gelation of α‐Lactalbumin‐Ovalbumin‐Mixed Gels

Legowo, Anang Mohamad; Imade, Tamotsu; Yasuda, Yukinori; Okazaki, Katsuichiro; Hayakawa, Shigeru

doi:10.1111/j.1365-2621.1996.tb14176.x

Cited by 10 publications

(12 citation statements)

References 26 publications

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“…The decreased accessibility of the disulfide bond will prohibit disulfide cross-linking during gelation. Legowo et al (40) observed that the addition of R-lac, a protein containing four disulfide bonds, significantly increased the hardness of heatset ovalbumin gels. This also confirms that the thiol group of ovalbumin is available for reaction and that the disulfide bonds in R-lac are accessible for reaction with the heat-exposed thiol groups of ovalbumin, in contrast to the one in ovalbumin.…”

Section: Resultsmentioning

confidence: 99%

“…This also confirms that the thiol group of ovalbumin is available for reaction and that the disulfide bonds in R-lac are accessible for reaction with the heat-exposed thiol groups of ovalbumin, in contrast to the one in ovalbumin. Indeed, Legowa et al (40) demonstrated the contribution of the Cys6-Cys120 disulfide bond of R-lac in the interaction between R-lac and ovalbumin. Note that WPI is a mixture of proteins.…”

Section: Resultsmentioning

confidence: 99%

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Acid-Induced Cold Gelation of Globular Proteins: Effects of Protein Aggregate Characteristics and Disulfide Bonding on Rheological Properties

Alting

Weijers

Hoog

et al. 2004

J. Agric. Food Chem.

107

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The process of cold gelation of ovalbumin and the properties of the resulting cold-set gels were compared to those of whey protein isolate. Under the chosen heating conditions, most protein was organized in aggregates. For both protein preparations, the aggregates consisted of covalently linked monomers. Both types of protein aggregates had comparable numbers of thiol groups exposed at their surfaces but had clearly different shapes. During acid-induced gelation, the characteristic ordering caused by the repulsive character disappeared and was replaced by a random distribution. This process did not depend on aggregate characteristics and probably applies to any type of protein aggregate. Covalent bonds are the main determinants of the gel hardness. The formation of additional disulfide bonds during gelation depended on the number and accessibility of thiol groups and disulfide bonds in the molecule and was found to clearly differ between the proteins studied. However, upon blocking of the thiol groups, long fibrillar structures of ovalbumin contribute significantly to gel hardness, demonstrating the importance of aggregate shape.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Acid-Induced Cold Gelation of Globular Proteins: Effects of Protein Aggregate Characteristics and Disulfide Bonding on Rheological Properties

Alting

Weijers

Hoog

et al. 2004

J. Agric. Food Chem.

107

View full text Add to dashboard Cite

show abstract

“…Thereafter, the MG‐like α‐La and reactive BSA can associate with each other to form irreversible complexes via hydrophobic bonding. Further heating may result in the formation of an adduct between these 2 whey proteins via a –SH/S–S bond interchange reaction, thus making a free –SH group available from the α‐La molecule (Cys6 or Cys120) (Legowo and others ). Additionally, 2 possible alternative reactions may occur after the formation of the reactive adduct.…”

Section: The Mechanism Of Whey Protein Aggregationmentioning

confidence: 99%

Stability of Whey Proteins during Thermal Processing: A Review

Wijayanti

Bansal

Deeth

2014

Comp Rev Food Sci Food Safe

297

186

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Whey proteins have many benefits due to their high nutritional value and their various applications in food products. A drawback of whey proteins is their instability to thermal processing, which leads to their denaturation, aggregation, and, under some conditions, gelation. As thermal processing is a major treatment in the processing of milk and milk products, its influence on whey proteins has been extensively studied. Understanding the mechanisms involved during each stage of denaturation and aggregation of whey proteins is critical to devising ways of improving their stability. These aspects are reviewed in this paper. Also covered are approaches to preventing or reducing heat-induced aggregation of whey proteins. Inhibition of aggregate formation has considerable potential for alleviating the problems that arise from the instability of whey proteins.

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“…This free thiol may react with BSA via -SH/S-S interchange reaction and form dimer, trimer, and so on. Free thiol of BSA may also involve in -SH/S-S interchange reaction with Cys6 or Cys120 of α -lactalbumin [ 34 , 35 ]. In a mix solution, BSA is more effective than β -lactoglobulin to react with α -lactalbumin because a more covalent disulfide bond is formed between BSA/ α -La than β -Lg/ α -La combination [ 19 , 34 ].…”

Section: Whey Protein-casein Complex Formation In Heated Milkmentioning

confidence: 99%

Heat-Induced Interaction of Milk Proteins: Impact on Yoghurt Structure

Asaduzzaman

Mahomud

Haque

2021

International Journal of Food Science

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Heating milk for yoghurt preparation has a significant effect on the structural properties of yoghurt. Milk heated at elevated temperature causes denaturation of whey protein, aggregation, and some case gelation. It is important to understand the mechanism involved in each state of stabilization for tailoring the final product. We review the formation of these complexes and their consequence on the physical, rheological, and microstructural properties of acid milk gels. To investigate the interactions between denatured whey protein and casein, the formation of covalent and noncovalent bonds, localization of the complexes, and their impact on ultimate gelation and final yoghurt texture are reviewed. The information regarding this fundamental mechanism will be beneficial to develop uniform quality yoghurt texture and potential interest of future research.

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Specific Disulfide Bond in α‐Lactalbumin Infiuences Heat‐ Induced Gelation of α‐Lactalbumin‐Ovalbumin‐Mixed Gels

Cited by 10 publications

References 26 publications

Acid-Induced Cold Gelation of Globular Proteins: Effects of Protein Aggregate Characteristics and Disulfide Bonding on Rheological Properties

Acid-Induced Cold Gelation of Globular Proteins: Effects of Protein Aggregate Characteristics and Disulfide Bonding on Rheological Properties

Stability of Whey Proteins during Thermal Processing: A Review

Heat-Induced Interaction of Milk Proteins: Impact on Yoghurt Structure

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