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Flow Properties of Chickpea Proteins
Author(s) -
LIU L.H.,
HUNG T.V.
Publication year - 1998
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1998.tb15715.x
Subject(s) - isoelectric point , shear thinning , chemistry , viscosity , apparent viscosity , rheology , chromatography , urea , aqueous solution , sodium , thermodynamics , biochemistry , organic chemistry , physics , enzyme
ABSTRACT Flow properties of aqueous chickpea protein dispersions were investigated. The dispersions had Newtonian flow behavior at concentrations up to 4%. Flow behavior became progressively less Newtonian as concentration increased above 4%. The apparent viscosity of the dispersions was pH and concentration dependent, being higher at the protein's most soluble pHs (pH 2 and 9) and lower at the isoelectric point (pH 4–5). Within the investigated temperatures (15, 25, 35 and 55°C), power law constants were unchanged up to 35°C but the flow behavior became non‐Newtonian at 55°C. Denaturation by urea and sodium dodecyl sulphate (SDS) increased the consistency index (m), casson yield stress and apparent viscosities, and the flow became more pseudoplastic with a decrease in the flow index (n).