2017
DOI: 10.1016/j.foodres.2017.08.059
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Formation of amyloid fibrils from soy protein hydrolysate: Effects of selective proteolysis on β-conglycinin

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Cited by 71 publications
(33 citation statements)
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“…Akkermans et al demonstrated the self-assembly fibrillation process was related to the changes in protein conformation and peptide hydrolysis, and peptides were the main building blocks of self-assembly fibrils [11]. e change in the average particle size indicated that the enzymatic hydrolysis did not significantly affect the minimum average particle size, which was consistent with the results of Xia et al [33]. We found a more interesting phenomenon; that is, the minimum average particle size of nanofibrils was between 100 nm and 150 nm.…”
Section: Particle Sizesupporting
confidence: 71%
“…Akkermans et al demonstrated the self-assembly fibrillation process was related to the changes in protein conformation and peptide hydrolysis, and peptides were the main building blocks of self-assembly fibrils [11]. e change in the average particle size indicated that the enzymatic hydrolysis did not significantly affect the minimum average particle size, which was consistent with the results of Xia et al [33]. We found a more interesting phenomenon; that is, the minimum average particle size of nanofibrils was between 100 nm and 150 nm.…”
Section: Particle Sizesupporting
confidence: 71%
“…These higher salt concentrations favor the extent of β‐sheet formation and disruption of tertiary and quaternary structures (Tang, Wang, & Huang, ). When β‐conglycinin is selectively hydrolyzed and removed from SPI by dialysis, the fibrils formed by heating the resulting SPI preparation for 60 min at 95 °C and pH 2.0 are long and semiflexible instead of short and worm‐like (Xia et al., ). The acidic subunits of glycinin form thin, long, and semiflexible fibrils when heated for 20 hr at 95 °C and pH 2.0 in contrast to the unordered amorphous aggregates of the basic subunits of glycinin formed under similar conditions.…”
Section: Legume Proteinsmentioning
confidence: 99%
“…However, since DH only indicates the proportion of cleaved peptide bonds, when the substrate is a multicomponent protein like soy protein, limited proteolysis can hardly control and determine which specific component or subunit of protein is being hydrolyzed. As a result, a novel method called selective proteolysis has been studied in recent years [ 9 , 10 , 11 , 12 ]. Differently from traditional proteolysis, selective proteolysis is more precise and controllable in terms of the acting sites, by which one can selectively and exclusively degrade a target component in soy protein without affecting the others.…”
Section: Introductionmentioning
confidence: 99%
“…Li et al [ 9 , 10 ] found that selectively hydrolyzing glycinin could facilitate soy protein to form interfacial films with high viscoelastic moduli, and thus its emulsifying properties improved. Our previous study found that decreasing the β-conglycinin component by selective proteolysis was beneficial to the formation of longer fibrils in the subsequent protein fibrillation process [ 12 ].…”
Section: Introductionmentioning
confidence: 99%