Work

Critical phosphate salt concentrations leading to altered micellar casein structures and functional intermediates

Year: 2019

Type: article

Abstract: We investigated the effect of different phosphate salts on the structural integrity of micellar casein (MC) at pH 7.0. With the increase of salt concentration, a reduction in turbidity was observed for the MC solutions, and it was modeled using an exponential decay function. The inflection point of the model was defined as the first critical salt concentration (C*), and it is suggested that the salt concentration initiates the disintegration of MC. For linear polyphosphates, C* decreased with the number of phosphate groups. Apparent viscosity (η app ) of MC solutions increased with the increase of salt concentration, and they recorded a peak while the turbidity decreased to a minimum. The salt concentration that resulted in the highest η app was identified as the second critical salt concentration (C**). It is hypothesized that the interactions among protein species present in the mixtures are at an optimum state at C**. Both C* and C** were found to be dependent on the MC concentration. The work presented herein supports an understanding of the concentration effect of phosphate salts on MC for structuring dairy products.

Source: Journal of Dairy Science

DOI: 10.3168/jds.2018-15746

Authors: Y. Saricay, C.A. Hettiarachchi, M.D. Culler, F.M. Harte

Institution: Pennsylvania State University

Language: English

Topic: Proteins in Food Systems

Subfield: Food Science

Field: Agricultural and Biological Sciences

Domain: Life Sciences

Open Access status: bronze

Funders: U.S. Department of Agriculture, National Institute of Food and Agriculture

Awards: G2479431890, G2968065326, G8279218188