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

Carpenter, John F.; Crowe, John H.

doi:10.1021/bi00435a044

Cited by 690 publications

(449 citation statements)

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“…Carpenter and Crowe [3] have shown that in the dry state, sugars interact with polar groups of globular proteins via hydrogen bonding. The competition between whey proteins/lactose interactions (hydrogen bonds) and lactose/lactose interactions (nucleation) might therefore reduce the propensity of lactose to crystallise.…”

Section: Discussionmentioning

confidence: 99%

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Lactose crystallisation and early Maillard reaction in skim milk powder and whey protein concentrates

Morgan

Nouzille

Baechler

et al. 2005

Lait

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-Lactose crystallisation and Maillard reaction are two major modifications occurring in milk and whey powders during processing and storage. In this work, the aim was first to monitor the solid-state early Maillard reaction (EMR) in whey protein concentrates (WPC) heated at 60 °C and various water activities, and then, to characterise the physical changes that occur as a consequence of heat treatment in skim milk powder (SMP) and WPCs. After a w adjustment, SMP and WPC were heated at 60 °C in hermetic conditions to induce an amino-sugar reaction. Furosine analysis (% of blocked lysine) was used to monitor the progress of EMR. The results showed that the kinetic of EMR was linked to the initial a w of the powders. Heating of SMP may lead to the crystallisation of lactose in humidified powders, without apparently affecting the progress of EMR. Surprisingly, lactose crystallisation -monitored by micro-Differential Scanning Calorimetry -was easily induced in heated SMP, whereas it was delayed or even inhibited in WPC. The results showed that this effect was dependent on the protein/lactose ratio in WPCs.lactose crystallisation / early Maillard reaction / whey protein concentrate / water activity Résumé -Cristallisation du lactose et réaction de Maillard précoce dans les poudres de lait écrémé et les concentrés de protéines du lactosérum. La cristallisation du lactose et la réaction de Maillard sont deux modifications importantes survenant au cours de la production et du stockage des poudres de lait et de lactosérum. L'objectif de ce travail était dans un premier temps de suivre la réaction de Maillard précoce (RMP) dans des concentrés de protéines de lactosérum (CPL) chauffés à 60 °C à différentes activités d'eau et, dans un deuxième temps, de caractériser les modifications physiques consécutives au traitement thermique (comparaison poudres de lait écrémé et CPL). Les poudres de lait écrémé et les CPL -équilibrés à différentes activités d'eau -étaient chauffés à 60 °C dans des conditions hermétiques pour induire la RMP (suivie par l'analyse de la furosine). Les résultats indiquaient que la cinétique de la RMP était liée à l'activité d'eau initiale de poudres. Dans les poudres de lait écrémé humidifiées et chauffées, la cristallisation du lactose ne semblait pas avoir d'impact sur l'évolution de la RMP. La microcalorimétrie différentielle à balayage permettait d'observer que la cristallisation du lactose, induite facilement dans les poudres de lait écrémé, était retardée voire inhibée dans les CPL. Les résultats indiquent que cet effet était dépen-dant du rapport protéine/lactose dans les CPL. cristallisation du lactose / réaction de Maillard précoce / concentré de protéines du lactosérum / activité de l'eau

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Section: Discussionmentioning

confidence: 99%

“…They proposed that the spatial organisation of proteins within the powder particle might account for this effect. Non-covalent interactions between protein and sugars in the dry state are known to occur via hydrogen bonding [3], and these interactions could also have an impact on the propensity of lactose to crystallise.…”

Section: Introductionmentioning

confidence: 99%

Lactose crystallisation and early Maillard reaction in skim milk powder and whey protein concentrates

Morgan

Nouzille

Baechler

et al. 2005

Lait

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“…The only exceptions are disaccharides. 16,80,81 FT-IR studies carried out with trehalose and proteins have confirmed that hydrogen bonding does occur between the sugar and the protein and that this is a requirement for the preservation of…”

Section: Solution Propertiesmentioning

confidence: 97%

Effect of trehalose on protein structure

Jain¹,

Roy²

2008

Protein Science

560

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Trehalose is a ubiquitous molecule that occurs in lower and higher life forms but not in mammals. Till about 40 years ago, trehalose was visualized as a storage molecule, aiding the release of glucose for carrying out cellular functions. This perception has now changed dramatically. The role of trehalose has expanded, and this molecule has now been implicated in a variety of situations. Trehalose is synthesized as a stress-responsive factor when cells are exposed to environmental stresses like heat, cold, oxidation, desiccation, and so forth. When unicellular organisms are exposed to stress, they adapt by synthesizing huge amounts of trehalose, which helps them in retaining cellular integrity. This is thought to occur by prevention of denaturation of proteins by trehalose, which would otherwise degrade under stress. This explanation may be rational, since recently, trehalose has been shown to slow down the rate of polyglutamine-mediated protein aggregation and the resultant pathogenesis by stabilizing an aggregation-prone model protein. In recent years, trehalose has also proved useful in the cryopreservation of sperm and stem cells and in the development of a highly reliable organ preservation solution. This review aims to highlight the changing perception of the role of trehalose over the last 10 years and to propose common mechanisms that may be involved in all the myriad ways in which trehalose stabilizes protein structures. These will take into account the structure of trehalose molecule and its interactions with its environment, and the explanations will focus on the role of trehalose in preventing protein denaturation.

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“…Several studies carried out by Timasheff and coworkers (9,18) show that sugars and polyols stabilize the folded structure of proteins in solution as a result of greater preferential hydration of the unfolded state compared with the native state. The mechanism is fundamentally different from stabilization in the dried state and points toward the different origins of protein denaturation under different stress conditions (17). In solution, trehalose has been observed to stabilize RNase A by increasing the surface tension of the medium, which leads to the preferential hydration of the protein (8,9).…”

mentioning

confidence: 99%

“…Sugars in general protect proteins against dehydration by hydrogen bonding to the dried protein by serving as water substitute (15,17). Several studies carried out by Timasheff and coworkers (9,18) show that sugars and polyols stabilize the folded structure of proteins in solution as a result of greater preferential hydration of the unfolded state compared with the native state.…”

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confidence: 99%

Why Is Trehalose an Exceptional Protein Stabilizer?

Kaushik¹,

Bhat

2003

Journal of Biological Chemistry

524

238

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Trehalose, a naturally occurring osmolyte, is known to be an exceptional stabilizer of proteins and helps retain the activity of enzymes in solution as well as in the freeze-dried state. To understand the mechanism of action of trehalose in detail, we have conducted a thorough investigation of its effect on the thermal stability in aqueous solutions of five well characterized proteins differing in their various physico-chemical properties. Among them, RNase A has been used as a model enzyme to investigate the effect of trehalose on the retention of enzymatic activity upon incubation at high temperatures. 2 M trehalose was observed to raise the transition temperature, T m of RNase A by as much as 18°C and Gibbs free energy by 4.8 kcal mol ؊1 at pH 2.5. There is a decrease in the heat capacity of protein denaturation (⌬C p ) in trehalose solutions for all the studied proteins. An increase in the ⌬G and a decrease in the ⌬C p values for all the proteins points toward a general mechanism of stabilization due to the elevation and broadening of the stability curve (⌬G versus T). A direct correlation of the surface tension of trehalose solutions and the thermal stability of various proteins has been observed. Wyman linkage analysis indicates that at 1.5 M concentration 4 -7 molecules of trehalose are excluded from the vicinity of protein molecules upon denaturation. We further show that an increase in the stability of proteins in the presence of trehalose depends upon the length of the polypeptide chain. The pH dependence data suggest that even though the charge status of a protein contributes significantly, trehalose can be expected to work as a universal stabilizer of protein conformation due to its exceptional effect on the structure and properties of solvent water compared with other sugars and polyols.Sugars have been known to protect proteins against loss of activity (1, 2), chemical (3, 4), and thermal denaturation (5-9). Among several sugars, ␣,␣-trehalose (␣-D-glucopyranosyl(131)-␣-D-glucopyranoside) has been known to be a superior stabilizer in providing protection to biological materials against dehydration and desiccation (10, 11). It is a compatible osmolyte that gets accumulated in organisms under stress conditions (12, 13). Because of this unique property, tremendous interest has been generated in understanding the molecular basis of stress management through induction of trehalose biosynthesis (13, 14).Trehalose has also been found to be very effective in the stabilization of labile proteins during lyophilization (15, 16) and exposure to high temperatures in solution (2,8,9). Sugars in general protect proteins against dehydration by hydrogen bonding to the dried protein by serving as water substitute (15, 17). Several studies carried out by Timasheff and coworkers (9,18) show that sugars and polyols stabilize the folded structure of proteins in solution as a result of greater preferential hydration of the unfolded state compared with the native state. The mechanism is fundamentally different from stabil...

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

Cited by 690 publications

References 39 publications

Lactose crystallisation and early Maillard reaction in skim milk powder and whey protein concentrates

Lactose crystallisation and early Maillard reaction in skim milk powder and whey protein concentrates

Effect of trehalose on protein structure

Why Is Trehalose an Exceptional Protein Stabilizer?

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