Abstract

Water structures in protein–water mixtures and cheeses were examined by Time Domain Reflectometry (TDR) and Nuclear Magnetic Resonance (NMR). The relaxation time obtained from TDR increased and the diffusion coefficient obtained from NMR decreased with increasing protein concentration, even if those physical quantities and time scales of respective observation techniques were considerably different. The correlation of these dynamic behaviors obtained from TDR and NMR is also found for water structures in cheeses. Fractal analysis of protein solutions by TDR measurements suggested that water structures in both systems were same with usual dispersion systems much more than solution systems. The fractal analysis with the τ–β diagram using geometric characteristics of the whole diagram is effective to characterize various water structures.

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