The stoichiometry of water sorption by proteins

Leeder, J. D.; Watt, I. C.

doi:10.1016/0021-9797(74)90169-6

Cited by 47 publications

(29 citation statements)

References 20 publications

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“…It is therefore insightful to compare the absorption isotherms from the mucus trails to those obtained from proteins in previous work reported elsewhere. For instance, a water sorption isotherm was obtained from lysozyme gravimetrically [34]. At lower RH values, the results were consistent with the predictions of a group-contribution model.…”

supporting

confidence: 75%

Water vapour sorption by the pedal mucus trail of a land snail

Lincoln

Simpson

Keddie

2004

Colloids and Surfaces B: Biointerfaces

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supporting

confidence: 75%

Water vapour sorption by the pedal mucus trail of a land snail

Lincoln

Simpson

Keddie

2004

Colloids and Surfaces B: Biointerfaces

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“…Previous studies have indicated the importance of hydrophilic groups in the binding of water molecules through hydrogen bond formation (44)(45)(46). Polymerization of gliadins via the formation of intermolecular disulfide bonds did not modify the moistureholding capacity of the films.…”

Section: Sds-page Analysis Sds-page Analysis Shown Inmentioning

confidence: 72%

Characterization of Biodegradable Films Obtained from Cysteine-Mediated Polymerized Gliadins

Hernández‐Muñoz

Kanavouras

Villalobos

et al. 2004

J. Agric. Food Chem.

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This study focuses on the effect exerted by interchain disulfide bonds on the functional properties of films made from gliadins when cross-linked with cysteine. Gliadins were extracted from commercial wheat gluten with 70% aqueous ethanol, and cysteine was added to the film-forming solution to promote cross-linking between protein chains. The formation of interchain disulfide bonds was assessed by SDS-PAGE analysis. Gliadin films treated with cysteine maintain their integrity in water and become less extensible while their tensile strength increases as a consequence of the development of a more rigid network. The glass transition temperature of cross-linked films shifts to slightly higher values. The plasticizing effects of glycerol and moisture are also demonstrated. The mechanical behavior of cysteine-cross-linked gliadin films was compared to that of polymeric glutenins. Cross-linked gliadins displayed tensile strength values similar to those of glutenin films but achieved slightly lower elongation values. Cysteine-cross-linked gliadin films present the advantage that they are ethanol soluble, facilitating film fabrication or their application as a coating for food or for any other film or surface.

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“…This amount is even lower than the calculated equivalent water monolayer value of 5.4%; these calculations assume the attachment of one water molecule per charged amino acid. 38 However, this approximation assumes that all charged amino acids are accessible to water vapor. Moreover, spray drying is a flash process, and therefore the obtained moisture contents do not reflect an equilibrium value.…”

Section: Resultsmentioning

confidence: 99%

Activity–stability considerations of trypsinogen during spray drying: Effects of sucrose

Tzannis¹,

Prestrelski²

1999

Journal of Pharmaceutical Sciences

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The preparation and processing of protein pharmaceuticals into powders may impose significant stresses that could perturb and ultimately denature them. In many cases their stabilization through added excipients is necessary to yield native and active proteins. In this study, the effect of spray drying on the structure and activity of a model protein (trypsinogen) was investigated. In the absence of excipients, spray drying resulted in small losses of its enzymatic activity. Protein conformational rearrangements in the solid state (observed via FTIR) and irreversible aggregation (upon reconstitution) constituted the major degradation pathways. The irreversible unfolding in the solid state was also confirmed by solution calorimetric studies that indicated a decreased thermal stability of the spray-dried protein after reconstitution. The presence of sucrose, a thermal and dehydration stress stabilizer, induced a concentration-dependent protective effect. Protein protection was afforded even at low carbohydrate concentrations, while at specific mass ratios (sucrose-to-protein = 1:1) complete activity preservation was achieved. However, at the high end of sucrose concentrations, a small destabilization was evident, indicating that excluded volume effects may be undesirable during preparation of protein microparticles via spray drying. The profile of both the protein conformational changes and thermal stability in the solid state closely followed that of the incurred activity losses, indicating that protein stabilization during dehydration is crucial during processing of these polypeptides.

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The stoichiometry of water sorption by proteins

Cited by 47 publications

References 20 publications

Water vapour sorption by the pedal mucus trail of a land snail

Water vapour sorption by the pedal mucus trail of a land snail

Characterization of Biodegradable Films Obtained from Cysteine-Mediated Polymerized Gliadins

Activity–stability considerations of trypsinogen during spray drying: Effects of sucrose

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