Self-assembly and Hydrogelation Properties of Peptides Derived from Peptic Cleavage of Aggregation-prone Regions of Ovalbumin
Egg white protein hydrolysate generated with pepsin was investigated for the presence of peptides with self-assembly and hydrogelation properties. Incubation of the hydrolysates for 16 h resulted in aggregates with significantly (<i>p</i> < 0.05) lower free amino nitrogen and sulfhydr...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2022-10-01
|
| Series: | Gels |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2310-2861/8/10/641 |
| _version_ | 1827617401933398016 |
|---|---|
| author | Raliat O. Abioye Caleb Acquah Pei Chun Queenie Hsu Nico Hüttmann Xiaohong Sun Chibuike C. Udenigwe |
| author_facet | Raliat O. Abioye Caleb Acquah Pei Chun Queenie Hsu Nico Hüttmann Xiaohong Sun Chibuike C. Udenigwe |
| author_sort | Raliat O. Abioye |
| collection | DOAJ |
| description | Egg white protein hydrolysate generated with pepsin was investigated for the presence of peptides with self-assembly and hydrogelation properties. Incubation of the hydrolysates for 16 h resulted in aggregates with significantly (<i>p</i> < 0.05) lower free amino nitrogen and sulfhydryl contents, and higher particle diameter and surface hydrophobicity compared to the hydrolysates. LC-MS/MS analysis of the aggregates resulted in identification of 429 ovalbumin-derived peptides, among which the top-six aggregation-prone peptides IFYCPIAIM, NIFYCPIAIM, VLVNAIVFKGL, YCPIAIMSA, MMYQIGLF, and VYSFSLASRL were predicted using AGGRESCAN by analysis of the aggregation “Hot Spots”. NIFYCPIAIM had the highest thioflavin T fluorescence intensity, particle diameter (5611.3 nm), and polydispersity index (1.0) after 24 h, suggesting the formation of β-sheet structures with heterogeneous particle size distribution. Transmission electron microscopy of MMYQIGLF, and VYSFSLASRL demonstrated the most favorable peptide self-assembly, based on the formation of densely packed, intertwined fibrils. Rheological studies confirmed the viscoelastic and mechanical properties of the hydrogels, with IFYCPIAIM, NIFYCPIAIM, VLVNAIVFKGL, and VYSFSLASRL forming elastic solid hydrogels (tan δ < 1), while YCPIAIMSA and MMYQIGLF formed viscous liquid-like hydrogels (tan δ > 1). The results provide valuable insight into the influence of peptide sequence on hydrogelation and self-assembly progression, and prospects of food peptides in biomaterial applications. |
| first_indexed | 2024-03-09T09:46:33Z |
| format | Article |
| id | doaj.art-12703e37672149dd80a8583c3c3720c6 |
| institution | Directory Open Access Journal |
| issn | 2310-2861 |
| language | English |
| last_indexed | 2024-03-09T09:46:33Z |
| publishDate | 2022-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Gels |
| spelling | doaj.art-12703e37672149dd80a8583c3c3720c62023-12-02T00:30:56ZengMDPI AGGels2310-28612022-10-0181064110.3390/gels8100641Self-assembly and Hydrogelation Properties of Peptides Derived from Peptic Cleavage of Aggregation-prone Regions of OvalbuminRaliat O. Abioye0Caleb Acquah1Pei Chun Queenie Hsu2Nico Hüttmann3Xiaohong Sun4Chibuike C. Udenigwe5Department of Chemistry and Biomolecular Sciences, Faculty of Science, University of Ottawa, Ottawa, ON K1N 6N5, CanadaSchool of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, Ottawa, ON K1H 8M5, CanadaDepartment of Chemistry and Biomolecular Sciences, Faculty of Science, University of Ottawa, Ottawa, ON K1N 6N5, CanadaDepartment of Chemistry and Biomolecular Sciences, Faculty of Science, University of Ottawa, Ottawa, ON K1N 6N5, CanadaSchool of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, Ottawa, ON K1H 8M5, CanadaDepartment of Chemistry and Biomolecular Sciences, Faculty of Science, University of Ottawa, Ottawa, ON K1N 6N5, CanadaEgg white protein hydrolysate generated with pepsin was investigated for the presence of peptides with self-assembly and hydrogelation properties. Incubation of the hydrolysates for 16 h resulted in aggregates with significantly (<i>p</i> < 0.05) lower free amino nitrogen and sulfhydryl contents, and higher particle diameter and surface hydrophobicity compared to the hydrolysates. LC-MS/MS analysis of the aggregates resulted in identification of 429 ovalbumin-derived peptides, among which the top-six aggregation-prone peptides IFYCPIAIM, NIFYCPIAIM, VLVNAIVFKGL, YCPIAIMSA, MMYQIGLF, and VYSFSLASRL were predicted using AGGRESCAN by analysis of the aggregation “Hot Spots”. NIFYCPIAIM had the highest thioflavin T fluorescence intensity, particle diameter (5611.3 nm), and polydispersity index (1.0) after 24 h, suggesting the formation of β-sheet structures with heterogeneous particle size distribution. Transmission electron microscopy of MMYQIGLF, and VYSFSLASRL demonstrated the most favorable peptide self-assembly, based on the formation of densely packed, intertwined fibrils. Rheological studies confirmed the viscoelastic and mechanical properties of the hydrogels, with IFYCPIAIM, NIFYCPIAIM, VLVNAIVFKGL, and VYSFSLASRL forming elastic solid hydrogels (tan δ < 1), while YCPIAIMSA and MMYQIGLF formed viscous liquid-like hydrogels (tan δ > 1). The results provide valuable insight into the influence of peptide sequence on hydrogelation and self-assembly progression, and prospects of food peptides in biomaterial applications.https://www.mdpi.com/2310-2861/8/10/641peptide self-assemblyegg white hydrolysatesovalbuminpeptide hydrogelsrheologybiomechanical properties |
| spellingShingle | Raliat O. Abioye Caleb Acquah Pei Chun Queenie Hsu Nico Hüttmann Xiaohong Sun Chibuike C. Udenigwe Self-assembly and Hydrogelation Properties of Peptides Derived from Peptic Cleavage of Aggregation-prone Regions of Ovalbumin Gels peptide self-assembly egg white hydrolysates ovalbumin peptide hydrogels rheology biomechanical properties |
| title | Self-assembly and Hydrogelation Properties of Peptides Derived from Peptic Cleavage of Aggregation-prone Regions of Ovalbumin |
| title_full | Self-assembly and Hydrogelation Properties of Peptides Derived from Peptic Cleavage of Aggregation-prone Regions of Ovalbumin |
| title_fullStr | Self-assembly and Hydrogelation Properties of Peptides Derived from Peptic Cleavage of Aggregation-prone Regions of Ovalbumin |
| title_full_unstemmed | Self-assembly and Hydrogelation Properties of Peptides Derived from Peptic Cleavage of Aggregation-prone Regions of Ovalbumin |
| title_short | Self-assembly and Hydrogelation Properties of Peptides Derived from Peptic Cleavage of Aggregation-prone Regions of Ovalbumin |
| title_sort | self assembly and hydrogelation properties of peptides derived from peptic cleavage of aggregation prone regions of ovalbumin |
| topic | peptide self-assembly egg white hydrolysates ovalbumin peptide hydrogels rheology biomechanical properties |
| url | https://www.mdpi.com/2310-2861/8/10/641 |
| work_keys_str_mv | AT raliatoabioye selfassemblyandhydrogelationpropertiesofpeptidesderivedfrompepticcleavageofaggregationproneregionsofovalbumin AT calebacquah selfassemblyandhydrogelationpropertiesofpeptidesderivedfrompepticcleavageofaggregationproneregionsofovalbumin AT peichunqueeniehsu selfassemblyandhydrogelationpropertiesofpeptidesderivedfrompepticcleavageofaggregationproneregionsofovalbumin AT nicohuttmann selfassemblyandhydrogelationpropertiesofpeptidesderivedfrompepticcleavageofaggregationproneregionsofovalbumin AT xiaohongsun selfassemblyandhydrogelationpropertiesofpeptidesderivedfrompepticcleavageofaggregationproneregionsofovalbumin AT chibuikecudenigwe selfassemblyandhydrogelationpropertiesofpeptidesderivedfrompepticcleavageofaggregationproneregionsofovalbumin |