A comparison between pressure and temperature effects on food constituents

Heremans,; Snauwaert,; Smeller,; Meersman,; Vermeulen, Pieter; Rubens,

doi:10.1201/9781420049008.ch15

Cited by 4 publications

(9 citation statements)

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“…The phase stability diagram of proteins may also be studied by infrared spectroscopy. For the enzyme lipoxygenase, Rubens (1999) found an excellent correlation between the changes in secondary structure and the inactivation of the enzyme as observed by Ludikhuyze et aI. (1998).…”

Section: Protein Unfolding and Denaturationsupporting

confidence: 74%

“…Surface activity-compressibility relationship of proteins at the air-water interface. Langmuir, 15, 1392-1399. Rubens, P. (1999.…”

Section: Resultsmentioning

confidence: 99%

“…The kinetics of hydrogen-deuterium exchange gives important information on the protein dynamics as shown by the dependence of the accessibility of the protein interior and its pressure and temperature dependence. A correlation is therefore found between the rate of hydrogendeuterium exchange from the changes in the amide II' region and the inactivation kinetics (Rubens, 1999).…”

Section: Protein Unfolding and Denaturationmentioning

confidence: 90%

“…Thus, it seems that the binding of urea at ambient pressure and the binding of water at high pressure may account for the negative activation energies that are observed in these processes. (1999), Rubens (1999) and the gelation of starch. In all cases, kinetic data are presented, although in a few cases a thermodynamic analysis is presented.…”

Section: Stability Phase Diagrams Of Food Macromoleculesmentioning

confidence: 99%

“…One of the practical consequences of this phenomenon is the stabilization against heat denaturation by low pressures. Not only has this been observed in several proteins and enzymes, but it also applies to the effect of pressure on the heat gelation of starch (Thevelein et al, 1981;Rubens et al, 1999). Of special interest is the observation that the inactivation kinetics of microorganisms results in diagrams similar to those of proteins (Sonoike et a1., 1992;Ludwig et a1., 1996).…”

mentioning

confidence: 99%

See 4 more Smart Citations

Ultra High Pressure Treatments of Foods

Hendrickx¹,

Knorr²,

Ludikhuyze³

et al. 2001

Food Engineering Series

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show abstract

Section: Protein Unfolding and Denaturationsupporting

confidence: 74%

“…Surface activity-compressibility relationship of proteins at the air-water interface. Langmuir, 15, 1392-1399. Rubens, P. (1999.…”

Section: Resultsmentioning

confidence: 99%

Section: Protein Unfolding and Denaturationmentioning

confidence: 90%

Section: Stability Phase Diagrams Of Food Macromoleculesmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Ultra High Pressure Treatments of Foods

Hendrickx¹,

Knorr²,

Ludikhuyze³

et al. 2001

Food Engineering Series

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Kinetic Study on the Changes in the Susceptibility of Egg White Proteins to Enzymatic Hydrolysis Induced by Heat and High Hydrostatic Pressure Pretreatment

Plancken

Delattre

Indrawati

et al. 2004

J. Agric. Food Chem.

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A kinetic study was conducted on the effect of heat pretreatment in the temperature range of 50-85 degrees C at atmospheric pressure and of high hydrostatic pressure pretreatment (100-700 MPa) at four temperatures (10, 25, 40, and 60 degrees C) on the susceptibility of egg white solutions (10% v/v, pH 7.6) to subsequent enzymatic hydrolysis by a mixture of trypsin and alpha-chymotrypsin at 37 degrees C and pH 8.0. Both heat pretreatment at atmospheric pressure and high-pressure pretreatment resulted in an increase in degree of hydrolysis (DH) after 10 min of enzymatic reaction (DH10) of egg white solutions, as measured using the pH-stat method, which could be described by a fractional conversion model (based on an apparent first-order reaction kinetic model). The temperature dependence of the corresponding rate constants could be described by the Arrhenius equation. At elevated pressure, a negative apparent activation energy was obtained, implying an antagonistic effect of pressure and temperature. The pressure dependence of the rate constants could be described by the Eyring equation, and negative activation volumes were observed, which demonstrates the positive effect of pressure on the susceptibility of egg white solutions to subsequent enzymatic hydrolysis.

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Changes in Sulfhydryl Content of Egg White Proteins Due to Heat and Pressure Treatment

Plancken

Loey

Hendrickx

2005

J. Agric. Food Chem.

170

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The sulfhydryl (SH) content of egg white proteins (10% v/v or 9.64 mg of protein/mL) after heat (50-85 degrees C) and combined heat- and high-pressure treatments (100-700 MPa, 10-60 degrees C) was determined using 5',5-dithiobis (2-nitrobenzoic acid) (DTNB), both for the soluble fraction and the total protein fraction. Only irreversible changes were taken into account. Both physical treatments were performed at two pH levels: pH 7.6, corresponding to the pH of fresh egg white, and pH 8.8, corresponding to that of aged egg white. Both heat and combined heat- and high-pressure treatment resulted in an exposure of buried SH groups. These exposed SH groups were involved in the formation of disulfide bond stabilized protein aggregates, as shown by gel electrophoresis. Under severe processing conditions (above 70 degrees C at atmospheric pressure or above 500-600 MPa, depending on the temperature applied), a decrease in total SH content could be observed, probably due to the formation of disulfide bonds by oxidation, especially at alkaline pH when the thiolate anion was more reactive. The high degree of exposure of sulfhydryl groups, and subsequent oxidation and sulfhydryl-disulfide bond exchange reactions resulting in soluble aggregates, can explain why pressure-induced egg white gels are softer and more elastic than heat-induced ones. When pressure treatment was performed at low temperatures (e.g., 10 degrees C), a lower pressure was required to induce similar changes in the sulfhydryl content, as compared to higher temperatures (e.g., 25 degrees C), indicating an antagonistic effect between pressure and temperature in the domain studied (10-60 degrees C, 100-700 MPa). Treatment conditions resulting in extensive protein insolubilization were accompanied by a transfer of free sulfhydryl groups from the soluble to the insoluble protein fraction. These SH groups were mainly accessible to DTNB.

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A comparison between pressure and temperature effects on food constituents

Cited by 4 publications

References 0 publications

Ultra High Pressure Treatments of Foods

Ultra High Pressure Treatments of Foods

Kinetic Study on the Changes in the Susceptibility of Egg White Proteins to Enzymatic Hydrolysis Induced by Heat and High Hydrostatic Pressure Pretreatment

Changes in Sulfhydryl Content of Egg White Proteins Due to Heat and Pressure Treatment

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