Thermal stability of skim milk/whey protein solution blends

Rattray, W.; Jelen, P.

doi:10.1016/s0963-9969(97)00056-2

Cited by 19 publications

(16 citation statements)

References 28 publications

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“…No 33.0 ± 0.4 20.4 ± 2.5 18.5 ± 5.0 17.9 ± 2.5 41.8 ± 9.9 9 20.8 ± 0.6 24.2 ± 0.5 22.1 ± 0.4 32.9 ± 0.7 16.7 ± 0.7 16.5 ± 0.9 15.5 ± 1.1 51.2 ± 1.6 10 19.0 ± 0.7 25.6 ± 0.2 22.7 ± 0.4 32.6 ± 0.4 11.6 ± 1.7 18.7 ± 1.3 15.7 ± 0.2 53.5 ± 2.8 a percentages are averages ± standard deviations from three methods: CONTINLL, CDSSTR, and SELCON 3 such changes were observed in the case of heated α-lactalbumin solutions. The explanation for this behaviour may reside in relatively weak hydrophobic interactions that occur between the unfolded molecules of β-lactalbumin (Rattray & Jelen 1998). Foegeding et al (1992) observed that the secondary structure of β-lactoglobulin heated at 72°C differed depending on whether it was dissolved in water or saline.…”

Section: Resultsmentioning

confidence: 99%

Changes of secondary structure and surface tension of whey protein isolate dispersions upon pH and temperature

Tomczyńska‐Mleko¹,

Kamysz²,

Sikorska³

et al. 2014

Czech J. Food Sci.

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Tomczyńska-Mleko M., Kamysz E., Sikorska E., Puchalski C., Mleko S., Ozimek L., Kowaluk G., Gustaw W., Wesołowska-Trojanowska M. (2014): Changes of secondary structure and surface tension of whey protein isolate dispersions upon pH and temperature. Czech J. Food Sci., 32: 82-89.The secondary structure of proteins in unheated and heated whey protein isolate dispersions and the surface tension of the solutions were investigated at different pH. Heating protein solutions at 80°C results in an increase of unordered structure. Nevertheless, the difference between the contents of unordered structure in the unheated and heated samples increases with increasing pH of the solution. At low protein concentrations the surface tension decreased with increasing protein concentration to about 5 mg/ml. For the heated solution, a similar trend was observed in the decrease in the surface tension with increasing concentrations of protein. In both cases, the curves depicting the surface tension as a function of protein concentration could be fitted to the exponential function with a negative exponent, but with the heated solutions lower values of surface tension were observed. Studies on the surface tension of whey protein isolate solutions prove that the unfolding of whey proteins, revealed by changes in the secondary structure, causes a decrease in the surface tension.

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Section: Resultsmentioning

confidence: 99%

Changes of secondary structure and surface tension of whey protein isolate dispersions upon pH and temperature

Tomczyńska‐Mleko¹,

Kamysz²,

Sikorska³

et al. 2014

Czech J. Food Sci.

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“…Grande parte dos trabalhos publicados sobre gelatinização das proteínas de CPS enfocou faixa de pH abaixo do ponto isoelétrico das proteínas do soro [7,16,22,23] ou acima [14,20,21,22,23]. Neste trabalho, foi escolhida à faixa correspondente ao pH das principais proteínas do CPS (4,0 e 5,2) para verificar seu comportamento quando aplicado na produção de alimentos ácidos, tais como iogurtes.…”

Section: Discussionunclassified

“…As proteínas do soro de leite que apresentam melhores propriedades gelatinizantes são a β-lactoglobulina e a albumina do soro bovino (BSA), mas sendo a primeira de 10 a 20 vezes mais abundante nos produtos com soro lácteo, pois ela é considerada a principal agente gelatinizante [1]. Essa propriedade deve-se a presença de grupos sulfidrilas livres [20].…”

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Perfil de textura e capacidade de retenção de água de géis ácidos de concentrado protéico de soro de leite

Antunes¹,

Motta²,

Antunes³

2003

Ciênc. Tecnol. Aliment.

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“…The solubility of a-La (10 g L À1 , pH 7.5) is equally high when heating at 65, 85 or 95 1C for 30 min at pH 7.5 (Bertrand-Harb et al, 2002). Rattray and Jelen (1997) measured the heat coagulation time (HCT) of a-La (1.7% w/w protein) at pH values from 6.45 to 6.70. The HCT represents the visual detection of large aggregate/floc formation for solutions heated at 140 1C.…”

Section: Article In Pressmentioning

confidence: 99%

“…The HCT represents the visual detection of large aggregate/floc formation for solutions heated at 140 1C. There was a sharp drop in the HCT from pH 6.7 to 6.6 and coagulation occured rapidly at pH 6.5 (Rattray & Jelen, 1997).…”

Section: Article In Pressmentioning

confidence: 99%