2.1. Hydration and Thermal Stability of a-Lactalbumin. A Calorimetrie Study

Rüegg, Max; Moor, U.; Lukesch, A.; Blanc, B.

doi:10.1515/9783110860719-007

Cited by 7 publications

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“…39 Hickey et al 40 measured the water activity of 32 Cheddars with different protein levels vacuum aged for 270 days and observed a signicant decrease of the water activity throughout the ripening process, primarily attributed to increased proteolysis. Besides, as illustrated in the study of Ruegg et al, 41 it was found that the decrease in water activity during ripening was less pronounced in Cheddar compared to both Emmental and Gruyere, which may explain the scoring trends of Cheddar and Comté and the discrimination between age groups. The variations in the reduction of water activity among different cheese varieties likely arise from the combined effects of varying moisture levels, ripening temperature, concentrations of proteolysis products, and the action of microorganisms on ripening.…”

Section: Analytical Methods Papermentioning

confidence: 83%

Chemometrics-driven monitoring of cheese ripening: a multimodal spectroscopic and scanning electron microscopy investigation

Abi-Rizk,

Jouan-Rimbaud Bouveresse,

Chamberland

et al. 2024

Anal. Methods

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Section: Analytical Methods Papermentioning

confidence: 83%

Chemometrics-driven monitoring of cheese ripening: a multimodal spectroscopic and scanning electron microscopy investigation

Abi-Rizk,

Jouan-Rimbaud Bouveresse,

Chamberland

et al. 2024

Anal. Methods

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The relation of ion pairs to protein hydration: An IR spectroscopic and X‐ray crystallographic survey

Poole¹,

Barlow²

1986

Biopolymers

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SynopsisWe report here a novel ir technique that we use to determine the apparent van't Hoffs energy for the distillation of water from protein amide and acid groups. The method is used to study the hydration properties of ten different proteins. The results show that water removal from the environment of ion-paired acid groups (those I 4 8, from a basic group on the protein surface) requires less energy than water removal from the environment of nonpaired acid groups. These observations are supported by an analysis of the solvent distributions in protein crystal structures. A model is proposed for the interaction between water and protein acid groups, and this model is used to account for the distributions and properties of certain eyelens proteins.

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Whey protein denaturation in heated milk and cheese whey

Hillier¹,

Lyster²

1979

Journal of Dairy Research

139

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Quantitative polyacrylamide gel electrophoresis has been used to measure residual native whey proteins remaining after heat treatment of skim-milk and cheese whey in a kinetic study. The denaturation of a-lactalbumin (a-la) appeared to be first order, but was probably a second-order reaction displaying pseudo firstorder kinetics. The denaturation of both yff-lactoglobulin A and B (/MgA and /MgB) followed second-order kinetics while that of serum albumin was more complex, and could equally well be described as first or second order. Equations are given relating log k x (in s-1 ) to temperature for a-la denaturation in skim-milk between 70 and 95 °C and between 100 and 150 °C. Similarly, equations relating log k 2 (in lg-1^-1 ) to temperature are given for /MgA in skim-milk between 100 and 150 °C, and for yff-lgB between 95 and 150 °C. The relative heat stability of /MgA and /MgB was found to vary.Below 95 °C /MgA appeared slightly more thermostable than /MgB in skim-milk, and the same was observed in cheese whey below 100 °C. Above these temperatures yff-lgB appeared more stable than /MgA. Denaturation of /MgB was only slightly more rapid in skim-milk than in whey at temperatures below 95 °C, but was significantly slower at higher temperatures.The recovery of residual protein from cheese whey is important to the dairy industry, and the denaturation of these whey proteins is therefore of considerable interest. However, the many studies which have been reported are often not directly comparable because of the variation in experimental technique and in the means used to express results. Kinetic data on rates of denaturation are rarely available, and then are not always in agreement. Lyster (1970), using immunochemical techniques, has measured the rates of denaturation of a-lactalbumin (a-la) and /Mactoglobulin (/?-lg) in heated milk, and found a-la to follow first-order kinetics, while /Mg followed second-order kinetics. Other workers have reported the denaturation of y#-lg as first order (Gough & Jenness, 1962). A rapid accurate measure of individual native whey proteins in complex mixtures is possible using polyacrylamide gel electrophoresis (PAGE) (Hillier, 1976;Darling & Butcher, 1976). This technique has been used for a comprehensive study of the kinetics of denaturation of the major proteins in milk and cheese whey over a wide range of temperatures.

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2.1. Hydration and Thermal Stability of a-Lactalbumin. A Calorimetrie Study

Cited by 7 publications

References 0 publications

Chemometrics-driven monitoring of cheese ripening: a multimodal spectroscopic and scanning electron microscopy investigation

Chemometrics-driven monitoring of cheese ripening: a multimodal spectroscopic and scanning electron microscopy investigation

The relation of ion pairs to protein hydration: An IR spectroscopic and X‐ray crystallographic survey

Whey protein denaturation in heated milk and cheese whey

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