Sequential hydration of a dry globular protein

Poole, P. L.; Finney, John

doi:10.1002/bip.360220135

Cited by 73 publications

(21 citation statements)

References 15 publications

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“…Silver and Karel (26) studied the behavior of invertase in model systems at low moisture contents, and found that the kinetics of sucrose hydrolysis in the low moisture region were best represented by a model in which water activity affects enzyme conformation, or diffusion resistance in a resistance shell in the immediate vicinity of the enzyme molecule. This entirely phenomenologically based interpretation of the kinetics receives strong support from a recent crystallographic study by Poole and Finney (22). These authors used direct difference IR and laser Raman spectroscopy to monitor sequential hydration of lysozyme.…”

Section: Enzyme Activity and Conformation Of Polymer Chainsmentioning

confidence: 91%

Effects of Water Activity and Water Content on Mobility of Food Components, and their Effects on Phase Transitions in Food Systems

Karel¹

1985

Properties of Water in Foods

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Section: Enzyme Activity and Conformation Of Polymer Chainsmentioning

confidence: 91%

Effects of Water Activity and Water Content on Mobility of Food Components, and their Effects on Phase Transitions in Food Systems

Karel¹

1985

Properties of Water in Foods

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“…Especially in the last several years, a growing number of food scientists from both academia and industry have increasingly recognized the practical significance of the glass transition as a Slade and Levine 1985, 1988a,b, 1991aGould and Christian 1988;Sapru and Labuza 1992a,b;Bolton et a/ 1993Bolton et a/ 1989Slade et al 1989;Myers-Betts and Baianu 1990;Oksanen and Zografi 1990;Ablett and Lillford 1991 ;Franks 1991a,b;Slade and Levine 1991a Cole et al 1983Levine and Slade 1986, 1988c,d, 1989c,d, 1990Blanshard and Van den Berg 1981Slade 1988a, 1989b;Lillford 1988;Cairault et al Franks 1987;Hirsh 1987;Franks 1989Franks , 1990Franks and Hatley 1990;Le Meste and Simatos 1990;Noel et 01 1990;Pika1 1990a,b;Belton 1991;Blond and Colas 1991;Chang and Baust 1991as;Franks and Van den Berg 1991 ; Franks et nl 1991 ; Lim and Reid 1991;Roos and Karel 1991f,g;Best 1992;Blond 1992;Caldwcll et al 1992;Chang and Randall 1992;Goff 1992;Goff et al 1992;Karel 1992;Nesvadba 1992a; Van den Berg 1992; Van den Berg et al 1992…”

Section: T and Methods Of Its Measurement In Foodsmentioning

confidence: 97%

“…As the name implies, water dynamics focuses on (i) the mobility (Chinachoti et al 1991b; Larsson 1991 ; Tanner et a1 1991 ; Goff 1992) and eventual 'availability' (Ablett and Lillford 1991 ; Franks 199 1 b) of the plasticizing diluent (be it water alone or an aqueous solution) ; and (ii) an interpretive approach to understanding how to control the mobility of the diluent in glass-forming food systems that would be inherently mobile, unstable and reactive at temperatures and moisture contents corresponding to the rubbery liquid state at T > (Slade and Levine 1991a). This concept (along with that of glass dynamics) has provided an innovative perspective on water relationships in foods Ablett and Lillford 1991 ;Franks 1991b;Goff 1992;Karel 1992;Nelson and Labuza 1992a;Roos 1992b; Table 3(B)), including, for example, moisture management and structural stabilization of IMF systems , 1988a and 'cryostabilization' of frozen, freezer-stored and freezedried aqueous glass-forming food materials and products (Cole el a1 1983Levine and Slade 1986, 1988a4, 1989a4, 1990. This perspective, the focal point of which is the critical importance of the glassy state phenomenon in foods, has received considerable recent support from many workers in the field (Table 10( A)).…”

Section: 'Water Dynamics' and 'Glass Dynamics'mentioning

confidence: 97%

The glassy state phenomenon in applications for the food industry: Application of the food polymer science approach to structure–function relationships of sucrose in cookie and cracker systems

Slade¹,

Levine²,

Ievolella³

et al. 1993

J Sci Food Agric

132

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This review of the glassy state phenomenon in applications for the food industry comprises two main parts. The first is a broad but brief overview of the so-called 'food polymer science' approach and its importance to food R&D studies of glassy solid and rubbery liquid states and glass transitions in food products and processes. The following elements of this approach are discussed: (i) the glass transition temperature (T,) and methods for its measurement in foods; (ii) plasticization by water and its effect on 6 ; (iii) the concepts of 'water dynamics' and 'glass dynamics' in non-equilibrium food systems; (iv) Williams-Landel Ferry kinetics in the rubbery state above T,, (v) state diagrams; and (vi) the effect of molecular weight on T,. A comprehensive and up-to-date listing of more than 400 literature references on the glassy state phenomenon and glass transitions in food materials and systems is featured in that part of the paper, and these references are also compiled and tabulated according to specific subject headings. The second part of this review highlights the application of the food polymer science approach in recently reported studies on the structure-function relationships of sucrose in cookie and cracker systems. This part describes (i) the sucrose-water state diagram as a tool in understanding cookie and cracker baking; (ii) shortcomings of the traditional AACC sugar-snap cookie method as a test-baking system, in contrast to a new test system based on a model commercial-type wire-cut cookie formula ; and (iii) a revealing illustration of sucrose functionality in cookie baking. The review concludes with a word about future prospects.

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“…This conclusion was supported by some hydrogen isotope-exchange studies (6,7) but contradicted by others (8). Raman (9)(10)(11) and solid-state NMR (12) studies have suggested significant (reversible) structural changes occurring in lysozyme upon lyophilization. Likewise, recent hydrogen isotope-exchange/high-resolution NMR (13) and FTIR (14,15) investigations of various proteins strongly point to lyophilization-induced reversible denaturation.…”

mentioning

confidence: 95%

Lyophilization-induced reversible changes in the secondary structure of proteins.

Griebenow

Klibanov

1995

Proc. Natl. Acad. Sci. U.S.A.

349

311

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Changes in the secondary structure of some dozen different proteins upon lyophilization of their aqueous solutions have been investigated by means of Fouriertransform infrared spectroscopy in the amide IHI band region. Dehydration markedly (but reversibly) alters the secondary structure of all the proteins studied, as revealed by both the quantitative analysis of the second derivative spectra and the Gaussian curve fitting of the original infrared spectra. Lyophilization substantially increases the ,8-sheet content and lowers the a-helix content of all proteins. In all but one case, proteins become more ordered upon lyophilization.Consider the common laboratory and bioindustrial process of lyophilization or freeze-drying of aqueous solutions of proteins. Suppose that this lyophilization is carried out such that no irreversible damage to the protein ensues-i.e., when the lyophilized protein is redissolved in water, it exhibits the same properties as prior to lyophilization. The question still remains whether the protein structure in the lyophilized form is native or whether the lyophilization has resulted in reversible protein denaturation. Apart from its biochemical interest, the answer has important biotechnological implications. For example, proteins that have been lyophilized (which is how research and pharmaceutical protein preparations are usually stored) undergo moisture-triggered aggregation (1). To understand the mechanism of this undesirable phenomenon and to develop rational strategies for its prevention, structural information on proteins in the solid-e.g., lyophilized-form is needed. In addition, lyophilized enzymes suspended in organic solvents have proven to be useful synthetic catalysts (2); enzyme structural data should help maximize their performance.The issue of protein conformation in the lyophilized form is controversial. For example, the results of Fourier-transform infrared (FTIR) spectroscopic investigations of hen egg-white lysozyme were interpreted to indicate that lysozyme structure in either aqueous solution or the lyophilized state is the same (3-6). This conclusion was supported by some hydrogen isotope-exchange studies (6, 7) but contradicted by others (8). Raman (9-11) and solid-state NMR (12) studies have suggested significant (reversible) structural changes occurring in lysozyme upon lyophilization. Likewise, recent hydrogen isotope-exchange/high-resolution NMR (13) and FTIR (14,15) investigations of various proteins strongly point to lyophilization-induced reversible denaturation.Recent advances, both instrumentational and conceptual, in FTIR spectroscopy make it a method of choice for examining the structure of solid proteins. This has been illustrated by the scholarly work of Prestrelski et al. (14,15), who have employed this methodology to quantify changes in the secondary structure of proteins caused by lyophilization. Using the second derivatives of the vibrational spectra of proteins in the amide I band region (1600-1720 cm-1), these authors have calculated so-call...

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Sequential hydration of a dry globular protein

Cited by 73 publications

References 15 publications

Effects of Water Activity and Water Content on Mobility of Food Components, and their Effects on Phase Transitions in Food Systems

Effects of Water Activity and Water Content on Mobility of Food Components, and their Effects on Phase Transitions in Food Systems

The glassy state phenomenon in applications for the food industry: Application of the food polymer science approach to structure–function relationships of sucrose in cookie and cracker systems

Lyophilization-induced reversible changes in the secondary structure of proteins.

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