Interactions Among Protein, Electrolytes and Water Determined by Nuclear Magnetic Resonance and Hydrodynamic Equilibria (Nmr)

Although salt is an important ingredient in meat products, water binding by muscle protein in the presence of salt has not been investigated. Biceps femoris muscle was dialyzed against distilled water and increasing levels of salt were added to seven aliquots. Sorption and desorption isotherm data at 5(DEGREES)C were obtained. Hysteresis was found only at a(,w) above 0.75 and the degree of hysteresis increased with salt content. Interaction of salt with protein was quantitatively determined in both sorption and desorption modes over a(,w) 0.75 to 0.93 as a function of total salt. Interaction was higher in the desorption mode. Interacted salt increased with salt content; a(,w) affected interaction, especially in the desorption mode.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Food Science

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2014

Author dc:creator

• Lioutas, Theodore Stergios

• Agriculture, Food Science and Technology

Identifier

(UMI)AAI8502222

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/70079