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Titolo:
Estimation of steric exclusion and differential interaction contributions to protein transfer free energies in aqueous cosolvent solutions
Autore:
McClements, DJ;
Indirizzi:
Univ Massachusetts, Dept Food Sci, Biopolymers & Colloids Res Lab, Amherst, MA 01003 USA Univ Massachusetts Amherst MA USA 01003 ds Res Lab, Amherst, MA 01003 USA
Titolo Testata:
FOOD HYDROCOLLOIDS
fascicolo: 4-6, volume: 15, anno: 2001,
pagine: 355 - 363
SICI:
0268-005X(200107/11)15:4-6<355:EOSEAD>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
THERMAL-DENATURATION; WHEY PROTEINS; RIBONUCLEASE-A; STABILIZATION; SUCROSE; STABILITY; EMULSIONS; MECHANISM; GELATION; WATER;
Keywords:
preferential interactions; proteins; cosolvents; transfer free energies;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: McClements, DJ Univ Massachusetts, Dept Food Sci, Biopolymers & Colloids Res Lab, Amherst, MA 01003 USA Univ Massachusetts Amherst MA USA 01003 erst, MA 01003 USA
Citazione:
D.J. McClements, "Estimation of steric exclusion and differential interaction contributions to protein transfer free energies in aqueous cosolvent solutions", FOOD HYDROC, 15(4-6), 2001, pp. 355-363

Abstract

The thermal stability, conformation and aggregation of globular proteins depend on the concentration and type of cosolvents present in the surrounding aqueous phase. The transfer free energy of proteins into cosolvent solutions provides a quantitative description of the influence of cosolvents on protein transitions between different states, e.g. folded vs. unfolded or aggregated vs. non-aggregated. An improved understanding of the physiochemical processes contributing to transfer free energies would facilitate the rational utilization of proteins as functional ingredients in compositionally complex foods. This paper describes a thermodynamic model for predicting steric exclusion and differential interaction (protein-dependent and protein-independent) contributions to protein transfer free energies in cosolvent solutions. The usefulness and limitations of the model are demonstrated by analyzing published protein transfer free energies. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 09:15:41