Publisher Summary Hydration can be considered a process of adding water incrementally to dry protein, until a level of hydration is reached beyond which further addition of water produces no change and only dilutes the protein. The hydration process has several stages and an end point, reflected similarly in different types of measurements. Time-average measurements appear to have a common pattern and most closely fit a single picture of the process. Dynamic measurements sometimes show a dependence on hydration level that lies outside the common pattern of the time-average results. The chapter summarizes the literature that bears on the protein hydration process and the hydration shell, categorized by type of measurement, and provides picture of the hydration process and the hydration shell and an assessment of the ways in which the hydration shell may modulate enzyme and other protein functions. The percolation model is discussed that focuses on the long-range connectivity established at a threshold coverage of a surface or volume with conducting or otherwise functional elements.

Protein hydration and function.

Fourier-transform infrared spectroscopy was used to characterize the interaction of stabilizing carbohydrates with dried proteins. Freeze-drying of trehalose, lactose, and myo-inositol with lysozyme resulted in substantial alterations of the infrared spectra of the dried carbohydrates. In the fingerprint region (900-1500 cm-1), there were large shifts in the frequencies of bands, a decrease in absorbance, and a loss of band splitting. These effects mimic those of water on hydrated trehalose. Bands assigned to hydroxyl stretching modes (around 3350 cm-1) were decreased in intensity and shifted to higher frequencies in the presence of the protein. In complementary experiments, it was found that dehydration-induced shifts in the positions of amide I and amide II bands for lysozyme could be partially and fully reversed, respectively, when the protein was freeze-dried in the presence of either trehalose or lactose. In addition, the carboxylate band, which was not detectable in the protein dried without the sugar, was apparent when these sugars were present. myo-Inositol was less effective at shifting the amide bands, and the carboxylate band was not detected in the presence of this carbohydrate. Also tested was the concentration dependency of the carbohydrates' influence on the position of the amide II band for dried lysozyme. The results showed that the ability of a given concentration of a carbohydrate to shift this band back toward the position noted with the hydrated protein coincided, at least in the extreme cases, with the capacity of that same level of carbohydrate to preserve the activity of rabbit skeletal muscle phosphofructokinase during freeze-drying.(ABSTRACT TRUNCATED AT 250 WORDS)

An infrared spectroscopic study of the interactions of carbohydrates with dried proteins.

Isokinetic relationship, isoequilibrium relationship, and enthalpy-entropy compensation.

Synthesis and magnetism of multi-dimensional cyanide-bridged bimetallic assemblies

There is abundant information concerning the functional behavior of whey proteins in model systems. The data on functional properties reported by different researchers, however, reveal wide discrepancies in values. For example, in the case of comparable whey preparations, apparent solubilities may range from 10 to 100%; strength of gels from 0.3 to greater than 10 N, foam overruns from 250 to 1500%, and foam stabilities from 0.5 to 30 min. Many of the data are of limited value in assessing the true functional characteristics of different preparations, treatments, or processing effects. Reports to date are useful in indicating the relative behavior of different proteins; however, the data do not always predict the performance of such proteins in actual food systems. This reflects the fact that in foods, extensive interactions with other components may occur, resulting in modified behavior of the proteins. Harper, (1984) has advocated the testing of these various preparations in simulated food systems which should validly relate the behavior to performance in commercial systems. Emphasis on standardization of specific protocols, with regard to order of addition in ingredients, temperature, pH control, and amount of energy input during mixing, homogenization, emulsification, etc. deserves serious consideration. While this approach is justifiable in terms of providing valuable data to commercial users, it does not minimize the importance of examining these proteins in model systems where the physicochemical basis of each functional attribute can be described in molecular terms (Kinsella, 1987). Such information is necessary to expedite appropriate methods of processing in order to control compositional variability, extent of denatauration, and possible protein modification. In addition, rapid, reliable tests for routine quality assurance that can provide practical information concerning functional applications would be of great value. Whey protein preparations vary immensely in functional behavior and are presently relegated to limited use as functional ingredients in the food industry. This need not be the case since conventional and new technologies permit rigorous control of production protocols, e.g., careful control of heat treatments can result in the production of whey protein preparations with consistent, reliable functional properties (deWit, 1981, 1984; Harper, 1984; Morr, 1985). As the market for functional proteins continues to expand, the whey industry must seek the means to refine whey protein products; determine useful functional properties; develop standardized manufacturing protocols; demonstrate the effectiveness of whey as a functional ingredient; promote, and then market, whey on the basis of performance at competitive cost.

Proteins in whey: chemical, physical, and functional properties

Differential scanning calorimetry (DSC) was used to study thermal transitions of the following whey proteins and enzymes in milk ultrafiltrate solution: β-lactoglobulin, α-lactalbumin, serum albumin, γ-globulin, apo- and Fe-lactoferrin, lysozyme, ribonuclease, α-chymotrypsin and xanthine oxidase. Denaturation enthalpies (ΔHD), denaturation temperatures (TD) and the half width of the denaturation peaks in DSC thermograms (ΔT½D) were determined and the degree of renaturation was estimated by rescanning previously denatured samples. A fair correlation between the results obtained by DSC and other more classical methods was found in general. However, for some proteins (α-lactalbumin, lysozyme, ribonuclease and xanthine oxidase), which have so far been considered relatively thermostable, calorimetry reveals conformational changes starting at temperatures as low as about 45 °C. In these cases thermostability observed after heat treatment of milk should be interpreted in terms of renaturation and not of high temperatures of denaturation.

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A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate

The fat globule size distribution in human milk

Structural chemistry of Prussian blue analogs. Single-crystal study of manganese(II) hexacyanocobaltate(III), Mn3[Co(DcN)6]2.xH2O

Hydration and thermal denaturation of β-lactoglobulin. A calorimetric study

The primary hydration process of native biopolymers is analyzed in a brief review of the literature, pertaining to various aspects of biopolymer–water systems. Based on this analysis, a hydration model is proposed that implies that the solution conformation of native biopolymers is stable at and above a critical degree of hydration (hp′ = 0.06–0.1 g H2O/g polymer). This water content corresponds to the fraction of strongly bound water, and amounts to ∼20% of the primary hydration sphere. In order to test this model, detailed sorption–desorption scanning experiments were performed on a globular protein (α-chymotrypsin). The results obtained are consistent with the proposed hydration model. They show that under certain experimental conditions, sorption isotherms can be obtained that do not exhibit hysteresis. These data represent equilibrium conditions and are thus accessible to thermodynamic treatment. Valid thermodynamic functions, pertinent to the interaction of water with biopolymers in their solution state, can be obtained from these sorption experiments.

Thermodynamic functions of biopolymer hydration. I. Their determination by vapor pressure studies, discussed in an analysis of the primary hydration process

Max Rüegg

Papers

A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate

The fat globule size distribution in human milk

Structural chemistry of Prussian blue analogs. Single-crystal study of manganese(II) hexacyanocobaltate(III), Mn3[Co(DcN)6]2.xH2O

Hydration and thermal denaturation of β-lactoglobulin. A calorimetric study

Thermodynamic functions of biopolymer hydration. I. Their determination by vapor pressure studies, discussed in an analysis of the primary hydration process