2014
DOI: 10.1016/j.foodhyd.2014.02.022
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Effect of calcium chloride on the structure and in vitro hydrolysis of heat induced whey protein and wheat starch composite gels

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Cited by 35 publications
(13 citation statements)
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“…At the same ion concentration, the electrostatic shielding effect of Na + was not as good as that of K + ion, which led to the relative enhancement of electrostatic repulsion of Na + -LMP/CAS complexes [ 1 ], and thus made larger particle size than K + -LMP/CAS complexes. It has been reported that Ca 2+ can promote the unfolding and aggregation of protein by enhancing hydrophobic interactions and forming a Ca 2+ bridge, thus prominently enhancing the particle size of the polysaccharide/protein complex [ 8 , 23 ]. Therefore, the particle size of Ca 2+ -LMP/CAS complexes was significantly larger than the Na + -LMP/CAS and K + -LMP/CAS complexes.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…At the same ion concentration, the electrostatic shielding effect of Na + was not as good as that of K + ion, which led to the relative enhancement of electrostatic repulsion of Na + -LMP/CAS complexes [ 1 ], and thus made larger particle size than K + -LMP/CAS complexes. It has been reported that Ca 2+ can promote the unfolding and aggregation of protein by enhancing hydrophobic interactions and forming a Ca 2+ bridge, thus prominently enhancing the particle size of the polysaccharide/protein complex [ 8 , 23 ]. Therefore, the particle size of Ca 2+ -LMP/CAS complexes was significantly larger than the Na + -LMP/CAS and K + -LMP/CAS complexes.…”
Section: Resultsmentioning
confidence: 99%
“…Many studies have reported the effects of single ions on the properties of the polysaccharide/protein complex, which showed that the formation of a polysaccharide/protein complex involves non-covalent interactions, mainly electrostatic interactions [ 8 , 9 ]. Salt ions affect the properties of the polysaccharide/protein complex [ 10 , 11 ] and partially shield the charges on these macromolecules and affect their interactions [ 12 ].…”
Section: Introductionmentioning
confidence: 99%
“…Many studies have reported the gelation properties of proteinstarch mixed system, which mainly focused on the investigation about the protein-starch interactions and heat induced gel properties of soy protein-cornstarch (Li, Yeh, & Fan, 2007), whey protein-wheat starch (Yang, Luan, Ashton, Gorczyca, & Kasapis, 2014), fish myofibrillar protein-cassava starch (Fan et al, 2017), and other types of proteins and starches. However, to the best of our knowledge, there were fewer researches on the gel properties of black bean proteincornstarch mixture.…”
mentioning
confidence: 99%
“…Increased calcium content has been linked to increased endogenous TGase activity and may be reason the “no starch gels” formed a consistent network. Calcium increased thermo‐stability of the protein gels by binding to the free carboxylic groups of aspartic and glutamic acids, thus triggering cross‐linking of proteins (Yang, Luan, Ashton, Gorczyca, & Kasapis, ).…”
Section: Resultsmentioning
confidence: 99%