Heat-Induced Interaction between Crude κ-Casein and β-Lactoglobulin

Long, J.E.; Winkle, Q. Van; Gould, I.A.

doi:10.3168/jds.s0022-0302(63)89276-0

Cited by 46 publications

(19 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Complex formation between b-lg and k-casein has been investigated in pure protein model systems (Zittle et al 1962;Long et al 1963;Sawyer et al 1963;Purkayastha et al 1967;Tessier et al 1969;McKenzie et al 1971 ;Euber & Brunner, 1982;Haque et al 1987), casein micelle model systems (Smits & van Brouwershaven, 1980;Singh & Fox, 1987;Jang & Swaisgood, 1990) and milk (Tessier et al 1969;Creamer et al 1978;Parnell-Clunies et al 1988).…”

mentioning

confidence: 99%

“…In many studies, the involvement of sulphydryl-disulphide interchange in the complex formation between b-lg and k-casein was shown by treatment with thiol-blocking reagents (Sawyer et al 1963;Purkayastha et al 1967), by zonal electrophoresis with and without reduction of disulphide bonds (Purkayastha et al 1967;Smits & van Brouwershaven, 1980;Parnell-Clunies et al 1988) or by using immobilized b-lg that was exposed to k-casein (Euber & Brunner, 1982 ;Jang & Swaisgood, 1990). Long et al (1963) presented evidence indicating that primary denaturation of b-lg precedes its interaction with k-casein. Although it was not demonstrated that the same products were formed, it was shown that only b-lg needed to be heated for an interaction to occur.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Heat-induced interactions of β-lactoglobulin A and κ-casein B in a model system

Cho

Singh

Creamer

2003

Journal of Dairy Research

View full text Add to dashboard Cite

The interaction of κ-casein and β-lactoglobulin is fundamental to all heat-induced modifications of milk product functionality, such as the heat stability of concentrated milks. Purified native κ-casein B and β-lg A solutions were heated at 80 °C at pH 6·7 separately and in a mixture. The circular dichroism spectra in the near UV indicated irreversible changes in the disulphide bonding patterns involving both proteins. Alkaline- and SDS-PAGE of heated samples showed that, in the presence of κ-casein, less β-lg was converted into β-lg polymers and the rate of loss of native β-lg was greater. When κ-casein was added to previously heated β-lg and the mixture was heated, the κ-casein reacted with the heat-induced β-lg polymers more readily than with the β-lg native monomers. The formation of β-lg dimers, trimers etc. was diminished. It was concluded that, when β-lg and κ-casein were heated together, β-lg formed thiol-exposed monomers, which reacted with each other or with the native κ-casein depending on the relative concentrations of β-lg and κ-casein. The products of these reactions included some disulphide-bonded 1[ratio ]1 β-lg[ratio ]κ-casein complexes, some monomer κ-casein and a range of large aggregates held together by either or both disulphide bonds and hydrophobic association.

show abstract

mentioning

confidence: 99%

mentioning

confidence: 99%

Heat-induced interactions of β-lactoglobulin A and κ-casein B in a model system

Cho

Singh

Creamer

2003

Journal of Dairy Research

View full text Add to dashboard Cite

show abstract

“…100 Hurt et al 104 clarified that increasing the temperature of MF from 50 to 65 °C could also cause denaturation of whey proteins and possible association with casein (CN) micelles. Long et al 105 reported that only 3.4% of β-Lactoglobulin was associated with κ-CN after 20 min at 65 °C, and thus when they was covalently associated, the yield of whey protein in the permeate would be reduced. In addition, aggregates of β-LG and α-LA have also been found when heated at 75 °C, 106 being unable to pass through the MF membrane.…”

Section: Predicting the Effect Of Microfiltration On The Properties Omentioning

confidence: 99%

Influence of Heat Treatment and Microfiltration on the Milk Proteins Properties

Verruck¹,

Sartor²,

Marenda³

et al. 2019

Adv Food Technol Nutr Sci Open J

View full text Add to dashboard Cite

Heat treatments are the established food technology for commercial processing of milk. However, degradation of valuable nutrients in milk (as proteins) and its sensory characteristics occur during these processes due to substantial heat exposure. The most important reactions that occur during milk heat treatment are the whey proteins denaturation, its interactions with the casein micelles and aggregation/dissociation of the casein micelles. Microfiltration represents an emerging food processing technology allowing gentle milk preservation at lower temperatures for similar, or better, nutritive value, microbial removal, and shelf stability. Thus, the aim of this work is to review the existing studies on the effects of microfiltration on milk proteins by comparing with the effects of heating treatments.

show abstract

“…For instance, heat treatment of 1: 1 mixture of 13-lactoglobulin and K-casein results in 3·4% 13-lactoglobulin interacting at 69°C, 82·7% at 85°C and 76·7% at 99°c. 76 Mixing ratios of the two proteins also influence complex formation. An increase in the proportion of 13-lactoglobulin results in a higher percentage of the protein interacting at 85°C.…”

Section: ~-Lactoglobulin-k-casein Interactionmentioning

confidence: 99%

“…Thus at mixing ratios 1: 1 and 3 : 1 the sedimentation coefficients are 44S and 48S respectively. 76 The size of the complex can be affected by heating the individual proteins prior to complexing. 32 The presence of inorganic salts affects the heat stability of milk through their action on the 13-lactoglobulin-K-casein complex.…”

Section: ~-Lactoglobulin-k-casein Interactionmentioning

confidence: 99%

Protein-Protein Interactions

Howell

1992

Biochemistry of Food Proteins

View full text Add to dashboard Cite

Heat-Induced Interaction between Crude κ-Casein and β-Lactoglobulin

Cited by 46 publications

References 13 publications

Heat-induced interactions of β-lactoglobulin A and κ-casein B in a model system

Heat-induced interactions of β-lactoglobulin A and κ-casein B in a model system

Influence of Heat Treatment and Microfiltration on the Milk Proteins Properties

Protein-Protein Interactions

Contact Info

Product

Resources

About