Enhancing the gelation of .beta.-lactoglobulin

Lee, Sam Pin.; Cho, Yunje.; Batt, Carl A.

doi:10.1021/jf00032a034

Cited by 24 publications

(16 citation statements)

References 35 publications

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“…In a recent publication, Lee et al (1993) stated that porcine /?-lg did not gel, but gave no experimental details. The present results confirmed that the free -SH group of /?-lg is important for thermal gelation of the protein and that porcine /?-lg, which is devoid of a free -SH group, was unable to form a thermal gel at pH 7 -0.…”

Section: Resultsmentioning

confidence: 99%

Porcine β-lactoglobulin does not undergo thermally induced gelation

Gallagher

Lynch

Mulvihill

1996

Journal of Dairy Research

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/?-Lactoglobulin (/?-lg) is the most abundant whey protein in bovine milk, comprising up to 50% of the total whey protein present. It consists of 162 amino acids with a calculated total mass of 18277 Da and contains two disulphide (-SS-) bonds, at Cys 66-Cys 160 and Cys 106-Cys 119 , and one free thiol (-SH) at Cys 121 , which is buried and unavailable for reaction in the native protein (Papiz et al. 1986). Above 55 °C progressive unfolding of the globular structure occurs which exposes the free-SH group and hydrophobic surfaces, allowing subsequent protein aggregation. Under suitable conditions of temperature, pH, salts and protein concentration, bovine /?-lg can form gels as a result of intermolecular protein-protein interactions such as hydrophobic, dipolar and electrostatic attractions, and covalent bond formation via-SH and-SS-interchange (Mulvihill & Kinsella, 1987). Porcine /?-lg contains 160 amino acids with a calculated total molecular mass of 17 8.11 Da. It has 79-6 % sequence homology at the cDNA level, and 66-9 % homology at the amino acid sequence level to bovine /?-lg (Alexander & Beattie, 1992). Porcine /?-lg contains two disulphide bonds but, in contrast to bovine /?-lg, it has no free-SH group (Kessler & Brew, 1970; Alexander & Beattie, 1992). In this study porcine /?-lg was used as a model protein to study the gelation of /?-lg devoid of a free-SH group.

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Section: Resultsmentioning

confidence: 99%

Porcine β-lactoglobulin does not undergo thermally induced gelation

Gallagher

Lynch

Mulvihill

1996

Journal of Dairy Research

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“…Gels formed from R40C/F82C BLG at 90°C have a strength five-fold greater than wild-type BLG supporting the existence of additional intermolecular disulfide linkages. 10 ) Since the concentration (0.075%) of BLG added to these yogurts was significantly below the minimum 6.8% required for the gelation of R40C/F82C, it appears that this BLG variant is complexing with other milk proteins to reduce syneresis. The additional free thiols in R40C/F82C may also promote intermolecular thioldisulfide interchange reactions enhancing the gelation of the other milk proteins.…”

Section: Discussionmentioning

confidence: 96%

“…R40C/F82C BLG was produced as described previously. 10) Reconstituted BLG-free skim milk. BLG-free skim milk was produced by ultrafiltration of raw skim milk.…”

Section: Methodsmentioning

confidence: 99%

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Reducing Whey Syneresis in Yogurt by the Addition of a Thermolabile Variant of β-Lactoglobulin

Lee

Kim

Watkins

et al. 1994

Bioscience, Biotechnology, and Biochemistry

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“…The addition of extra thiol groups to β-LG either by chemical thiolation (Kim et al 1990) or genetic engineering (Lee et al 1993) dramatically increases their ability to polymerise through thiol/disulphide exchange or oxidation. Conversely, it is also possible to generate a thiol-free mutant of bovine β-LG (Jayat et al 2004) or to use thiol-free porcine β-LG (Gallagher and Mulvihill 1997) in order to reduce disulphide polymerisation.…”

Section: Structure and Mechanical Properties Of Acid Dairy Gelsmentioning

confidence: 99%

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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Enhancing the gelation of .beta.-lactoglobulin

Cited by 24 publications

References 35 publications

Porcine β-lactoglobulin does not undergo thermally induced gelation

Porcine β-lactoglobulin does not undergo thermally induced gelation

Reducing Whey Syneresis in Yogurt by the Addition of a Thermolabile Variant of β-Lactoglobulin

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

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