Role of Sulfhydryl Groups in the Interaction of κ-Casein and β-Lactoglobulin

Sawyer, William H.; Coulter, S.T.; Jenness, Robert

doi:10.3168/jds.s0022-0302(63)89096-7

Cited by 74 publications

(37 citation statements)

References 11 publications

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“…Non-covalent interactions and disulfide bonds (via thiol-disulfide exchange reactions) are known to be involved in the interactions. Early studies showed that there were specific reactions between κ-CN on the casein micelle surface and denatured β-LG, and that these reactions involved thiol-disulfide exchange Sawyer, Coulter, & Jenness, 1963). Recent studies have shown that the interactions of the denatured whey proteins with the casein micelles are strongly pH dependent (Anema & Klostermeyer, 1997;Anema & Li, 2003a,b;Anema, Lowe et al, 2004).…”

Section: Whey Protein Interactions With the Casein Micellesmentioning

confidence: 97%

Interactions of milk proteins during heat and high hydrostatic pressure treatments — A Review

Considine

Patel

Anema

et al. 2007

Innovative Food Science & Emerging Technologies

295

194

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Section: Whey Protein Interactions With the Casein Micellesmentioning

confidence: 97%

Interactions of milk proteins during heat and high hydrostatic pressure treatments — A Review

Considine

Patel

Anema

et al. 2007

Innovative Food Science & Emerging Technologies

295

194

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“…These differences in mechanism of complexation presumably influence the solubility properties of isolates prepared from milks heated at different pH values. As heat-induced interaction between 8-lactoglobulin and x-casein is prevented by the sulphydryl blocking agent N-ethylmaleimide (NEM) (Sawyer, Coulter & Jenness, 1963) and disrupted by adding R-mercaptoethanol (Snoeren & van der Spek, 1977), it is now widely accepted that disulphide linkage is involved in the interaction. To determine the contribution of disulphide linkage to heat-induced casein-whey protein interactions at different pH values, pH 4.6 precipitable nitrogen was measured after heating milk at different pH values in the presence and absence of 50 mM NEM.…”

Section: Solubility Of Protein Isolatesmentioning

confidence: 99%

Proteins recovered from milks heated at alkaline pH values

Grufferty

Mulvihill

1987

Int J of Dairy Tech

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Approximately 95% of available nitrogen can be precipitated from milk on adjustment to pH 4.6 after heating at 90°C × 15 minutes at its natural pH and pH 7.5, while 89% can be precipitated after heating at pH 10.0 at 60°C × 3 minutes. Non‐recovered protein includes some serum albumin, β‐lactoglobulin, α‐lactalbumin and proteose peptones. Protein isolates precipitated from milk heated at pH >7.0 are more soluble in the pH range 6.0–7.0 than those precipitated from milk heated at its natural pH. Whey proteins complex onto the casein micelles after heating milk at its natural pH, while on heating at pH >7.0 whey proteins appear to interact with k‐casein in the serum phase. When N‐ethylmaleimide is present in milk during heating the percentage protein recovered on pH 4.6 precipitation is decreased, confirming that disulphide linkage is involved in complex formation. However, addition of β‐mercaptoethanol to recovered isolates did not result in dissociation of the casein/whey protein complex, suggesting that forces other than disulphide bonding are also involved in maintaining the complex.

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“…Whey proteins are also highly susceptible to heat treatment and are found to denature between 60 and 70 °C. This temperature‐induced denaturation of β‐lactoglobulin exposes the free sulfhydryl group, which has the capability of crosslinking with other β‐lactoglobulin and κ‐casein molecules via disulfide bonds (Sawyer and others 1963; Wong and others 1996). NDM and whey protein concentrate (WPC), if used in a process cheese formula, may contribute to increased levels of whey protein in the process cheese.…”

mentioning

confidence: 99%

Process Cheese: Scientific and Technological Aspects—A Review

Kapoor¹,

Metzger²

2008

Comp Rev Food Sci Food Safe

243

203

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Process cheese is produced by blending natural cheese in the presence of emulsifying salts and other dairy and nondairy ingredients followed by heating and continuous mixing to form a homogeneous product with an extended shelf life. Extensive research on the important physicochemical and functional properties associated with process cheese and the various physicochemical, technological, and microbiological factors that influence these properties has resulted in process cheese being one of the most versatile dairy products with numerous end-use applications. The present review is an attempt to cover the scientific and technological aspects of process cheese and highlight and critique some of the important research findings associated with them. The 1st objective of this article is to extensively describe the physicochemical properties and microstructure, as well as the functional properties, of process cheese and highlight the various analytical techniques used to evaluate these properties. The 2nd objective is to describe the formulation parameters, ingredients, and various processing conditions that influence the functional properties of process cheese. This review is primarily targeted at process cheese manufacturers as well as students in the field of dairy and food science who may want to learn more about the scientific and technological aspects of process cheese. The review is limited to the relevant research associated with process cheeses as defined by the U.S. Code of Federal Regulations and does not cover imitation and substitute cheeses.

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Role of Sulfhydryl Groups in the Interaction of κ-Casein and β-Lactoglobulin

Cited by 74 publications

References 11 publications

Interactions of milk proteins during heat and high hydrostatic pressure treatments — A Review

Interactions of milk proteins during heat and high hydrostatic pressure treatments — A Review

Proteins recovered from milks heated at alkaline pH values

Process Cheese: Scientific and Technological Aspects—A Review

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