2022
DOI: 10.1016/j.foodhyd.2021.107378
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Buckwheat self-assembling peptide-based hydrogel: Preparation, characteristics and forming mechanism

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Cited by 30 publications
(32 citation statements)
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“…Future studies on determination of thiol (SH) and disulfide bond (S–S) could be helpful to understand the role of covalent interactions in the gel formation of QPI hydrolysates. Determining peptide sequences using LC-MS/MS and evaluating their aggregation and gelation tendencies using computational tools ( Yu et al, 2022 ) will further elucidate the gelation mechanism. This study also provides a new route to fabricate thermally induced QPI gels via enzymatic hydrolysis for potential industrial production of food products such as sausages, meat substitutes, and tofu-like products.…”
Section: Discussionmentioning
confidence: 99%
“…Future studies on determination of thiol (SH) and disulfide bond (S–S) could be helpful to understand the role of covalent interactions in the gel formation of QPI hydrolysates. Determining peptide sequences using LC-MS/MS and evaluating their aggregation and gelation tendencies using computational tools ( Yu et al, 2022 ) will further elucidate the gelation mechanism. This study also provides a new route to fabricate thermally induced QPI gels via enzymatic hydrolysis for potential industrial production of food products such as sausages, meat substitutes, and tofu-like products.…”
Section: Discussionmentioning
confidence: 99%
“…HSSC was thawed at room temperature. The amino acids of HSSC were determined according to Yu et al 18 HSSC was dispersed in Milli-Q water (1:100, w/v) and hydrolyzed in a shaking bath with alkaline protease (pH 9.0, 50 °C), neutral protease (pH 7.0, 37 °C), bromelain (pH 7.5, 50 °C), papain (pH 6.0, 37 °C), and trypsin (pH 7.0, 37 °C). Enzymes were added to the solution at a ratio of 300 U/g (enzyme/protein) to initiate.…”
Section: ■ Materials and Methodsmentioning
confidence: 99%
“…In the process of movement, peptides assemble in an irregular manner. Following that, hydrophobic and other interactions drive peptides to permute orderly and eventually shape a hydrogel (Criado-Gonzalez et al, 2020;Ruter et al, 2020;Yu et al, 2022). For example, MAX1 peptide, which in aqueous solution offers a hydrophobic interface of valine (V) residues and a hydrophilic interface of lysine (K) residues, conducted lateral assembly through hydrophobic interaction among side chains, finally generating a noncovalent crosslinking network (Lin et al, 2011).…”
Section: Hydrophobic Interactionmentioning
confidence: 99%
“…Although tetrapeptides are the most common structure, dipeptides and tripeptides can form β-turn as well (Boussard and Marraud, 1985). Yu et al described how the secondary structure of peptides realized the transformation from βsheet to α-helix and β-turn in the process of SAPH formation, and βturn was pivotal to stabilizing the SAPH (Yu et al, 2022).…”
Section: Formation Of Self-assembling Peptide Hydrogelsmentioning
confidence: 99%
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