Thermodynamic analysis of the impact of the surfactant-protein interactions on the molecular parameters and surface behavior of food proteins

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Thermodynamic analysis of the impact of the surfactant-protein interactions on the molecular parameters and surface behavior of food proteins
Engineering Village 2
? 2006 Elsevier Inc
Accession number: 06059678369

Title: Thermodynamic analysis of the impact of the surfactant-protein interactions on the molecular parameters and surface behavior of food proteins

Authors: Semenova, Maria G.; Belyakova, Larisa E.; Polikarpov, Yurii N.; Il'in, Michael M.; Istarova, Tatyana A.; Anokhina, Maria S.; Tsapkina, Elena N.

Author affiliation: Institute of Biochemical Physics, Russian Academy of Sciences, 119991 Moscow, Russian Federation

Serial title: Biomacromolecules

Abbreviated serial title: Biomacromolecules

Volume: v 7

Issue: n 1

Issue date: January 2006

Publication year: 2006

Pages: p 101-113

Language: English

ISSN: 1525-7797

CODEN: BOMAF6

Document type: Journal article (JA)

Publisher: American Chemical Society, Columbus, OH 43210-3337, United States

Abstract: This paper reports on the thermodynamics of the interactions between surfactants (anionic, CITREM, SSL; nonionic, PGE; zwitterionic, phospholipids) and food proteins (sodium caseinate, legumin) depending on the chemical structure and molecular state (individual molecules, micelles) of the surfactants and the molecular parameters (conformation, molar mass, charge) of the proteins under changes of pH in the range from 7.2 to 5.0 and temperature from 293 to 323 K. The marked effect of the protein-surfactant interactions on the molecular parameters (the weight-average molar mass, the gyration and hydrodynamic radii) and the thermodynamic affinity of the proteins for an aqueous medium were determined by a combination of static and dynamic laser light scattering. Thermodynamically justified schematic sketches of the molecular mechanisms of the complex formation between like-charged proteins and surfactants have been proposed. In response to the complex formation between the proteins and the surfactants, the more stable and fine foams have been detected generally. ? 2006 American Chemical Society.

Number of references: 62

Ei main heading: Proteins

Ei controlled terms: Surface active agents - Molecules - Thermodynamic properties - Structure (composition) - Molecular structure - pH effects - Thermal effects - Light scattering - Laser applications - Differential scanning calorimetry

Uncontrolled terms: Food proteins - Surfactant-protein interactions - Molecular parameters - Thermodynamic analysis - Laser light scattering

Ei classification codes: 804.1 Organic Compounds - 803 Chemical Agents and Basic Industrial Chemicals - 931.3 Atomic & Molecular Physics - 641.1 Thermodynamics - 801.4 Physical Chemistry - 801.1 Chemistry, General

Treatment: Experimental (EXP)

DOI: 10.1021/bm050455m

Database: Compendex

Compilation and indexing terms, ? 2006 Elsevier Inc. All rights reserved
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