Access to this article is restricted until 24 months after publication by request of the publisher.. Restriction lift date: 2022-01-30
Water sorption and hydration properties of high protein milk powders are influenced by enzymatic crosslinking and calcium chelation
Loading...
Files
Accepted Version
Supplementary Data
Date
2020-01-30
Authors
Power, Orla M.
Maidannyk, Valentyn
McSweeney, David J.
Fenelon, Mark A.
O'Mahony, James A.
McCarthy, Noel A.
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier B.V.
Published Version
Abstract
Calcium chelating agents, such as sodium hexametaphosphate (SHMP), can be added to milk protein (MPC) solutions to aid in rehydration; however, this leads to a concomitant increase in solution viscosity due to micelle swelling/dissociation. Crosslinking casein proteins in MPC using transglutaminase (TGase) can help retain casein micelle structure and maintain low viscosity. This study aimed to determine the water sorption and hydration properties of MPC powders, as influenced by the crosslinking of milk proteins and the addition of SHMP. Crosslinked casein protein (TG-MPC) powders without SHMP addition had improved wettability, water sorption and water diffusion compared to the non-crosslinked control (C-MPC) powder. All powders containing SHMP were found to have increased water sorption compared to control powders without SHMP addition. Powder dissolution data showed that increasing SHMP content increased powder particle size, compared to powders without SHMP addition, indicating increased powder particle swelling due to increased water uptake.
Description
Keywords
Milk protein concentrate , Sodium hexametaphosphate , Transglutaminase , Powder rehydration , Calcium
Citation
Power, O. M., Maidannyk, V., McSweeney, D. J., Fenelon, M. A., O'Mahony, J. A. and McCarthy, N. A. (2020) 'Water sorption and hydration properties of high protein milk powders are influenced by enzymatic crosslinking and calcium chelation', Powder Technology. doi: 10.1016/j.powtec.2020.01.075