Gelation behaviour and gel properties of the 7S and 11S globulin protein fractions from faba bean (Vicia faba var. minor) at different NaCl concentrations
M. Johansson, Saeid Karkehabadi, Daniel Johansson, Maud Langton
Food Hydrocolloids
Abstract
The 7S and 11S globulins, the main protein fractions found in legumes, may differ in functionality. This study evaluated gel formation and rheological and microstructural properties of gels formed from the 7S and 11S protein fractions of faba bean. The effect of adding sodium chloride (NaCl) was also investigated. In terms of rheological and mechanical properties, NaCl addition appeared to have an opposing effect on 7S and 11S gels. Gels formed from 7S showed increases in storage modulus and peak stress when NaCl was added, whereas gels formed from 11S showed decreases. Microstructural changes were observed only for 7S gels, for which addition of NaCl resulted in transition from a fine-stranded to a coarse-stranded gel network. The 11S gels showed a fine-stranded gel network at all NaCl concentrations investigated. Gels formed from a mixture of 7S and 11S (7S:11S ratio 3:7) showed similar rheological properties and microstructure as the 11S gels.
Extracted Claims
5 claims extracted from this paper into the knowledge graph
mixture of 7S and 11S globulin protein fractions (7S:11S ratio 3:7) shows similar rheological properties and microstructure as 11S gels
“Gels formed from a mixture of 7S and 11S (7S:11S ratio 3:7) showed similar rheological properties and microstructure as the 11S gels.”
11S globulin protein fraction maintains fine-stranded gel network
“The 11S gels showed a fine-stranded gel network at all NaCl concentrations investigated.”
7S globulin protein fraction increases storage modulus and peak stress
“Gels formed from 7S showed increases in storage modulus and peak stress when NaCl was added”