2022
DOI: 10.1016/j.procbio.2022.03.012
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Effect of enzymatic hydrolysis followed after extrusion pretreatment on the structure and emulsibility of soybean protein

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Cited by 29 publications
(10 citation statements)
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“…Certainly, the extrusion-associated physicochemical changes at the protein level include not only a decreased protein dispersibility index and an increase in beta-sheet structure, which indicates reduced solubility and potential protein aggregation, but also an increase in protein digestibility [ 16 ]. In this context, extrusion makes proteins more accessible to peptide bond cleavage by gastrointestinal enzymes [ 16 , 38 , 39 ], which in turn could improve the protein quality parameter protein digestibility-corrected amino acid score as the content of limiting amino acids in chickpea protein hardly differs before and after extrusion [ 21 ]. Furthermore, protein denaturation and aggregation make them more susceptible to enzymatic hydrolysis due to the target sites becoming more exposed [ 40 ].…”
Section: Resultsmentioning
confidence: 99%
“…Certainly, the extrusion-associated physicochemical changes at the protein level include not only a decreased protein dispersibility index and an increase in beta-sheet structure, which indicates reduced solubility and potential protein aggregation, but also an increase in protein digestibility [ 16 ]. In this context, extrusion makes proteins more accessible to peptide bond cleavage by gastrointestinal enzymes [ 16 , 38 , 39 ], which in turn could improve the protein quality parameter protein digestibility-corrected amino acid score as the content of limiting amino acids in chickpea protein hardly differs before and after extrusion [ 21 ]. Furthermore, protein denaturation and aggregation make them more susceptible to enzymatic hydrolysis due to the target sites becoming more exposed [ 40 ].…”
Section: Resultsmentioning
confidence: 99%
“…This indicated that the secondary structure of TM unwound and became loose and disordered under gastrointestinal digestion, 47 which may provide more enzyme cleavage sites for TM, making it easier to be degraded by digestive enzymes and generate a large number of smaller peptides. 48 Molecular force is an essential indicator to measure the interactions between protein molecules. 49 The ionic bonds, hydrogen bonds, and disulfide bonds in the digested TM were significantly reduced, while the hydrophobic interactions were significantly increased (p < 0.05) (Figure 5F).…”
Section: ■ Results and Discussionmentioning
confidence: 99%
“…The content of β-sheet and β-turn increased to 17.1 and 21.9%, respectively. This indicated that the secondary structure of TM unwound and became loose and disordered under gastrointestinal digestion, which may provide more enzyme cleavage sites for TM, making it easier to be degraded by digestive enzymes and generate a large number of smaller peptides …”
Section: Resultsmentioning
confidence: 99%
“…This may be because the HPH shear force exposed the SPC hydrophobic groups originally hidden in the folded structure, making the structure of the protein more flexible and H 0 increased ( 35 ). However, when the HP is too high, the decrease of surface hydrophobicity may be because the increased shear force will lead to the aggregation of proteins through hydrophobic interaction, and the protein aggregates cover the hydrophobic water points on the protein surface, which limits the binding with ANS and reduces the surface hydrophobicity of proteins ( 36 ). The results showed that the HPH opened the protein structure after enzymatic hydrolysis and changed the exposure degree of hydrophobic groups, thus leading to the change of H 0 .…”
Section: Results and Analysismentioning
confidence: 99%