Academic Journal
Effect of pH on the Formation, Disintegration and Antioxidant Activity of Mung Bean Protein Fibrils.
| Τίτλος: | Effect of pH on the Formation, Disintegration and Antioxidant Activity of Mung Bean Protein Fibrils. |
|---|---|
| Συγγραφείς: | Tian, Yike, Zhang, Shuning, Huang, Weining, Li, Ning, Liang, Li |
| Πηγή: | Antioxidants; Dec2025, Vol. 14 Issue 12, p1399, 15p |
| Θεματικοί όροι: | Hydrogen-ion concentration, Antioxidants, Protein structure, Bioactive compounds, Plant proteins, Peptides, Microfibrils, Hydrolysis |
| Περίληψη: | Protein fibrils are highly ordered structures. Mung bean protein (MBP) fibrils were fabricated after heating under acidic condition. The formation mechanism, structural variety and antioxidant capacities of mung bean protein fibrils were investigated under different pH conditions. The fibrillation process was characterized by extensive hydrolysis of MBP into low-molecular-weight peptides, which subsequently self-assembled into fibrils with increasing contour length over time. The formed fibrils exhibited a dominant β-sheet structure but demonstrated high sensitivity to pH changes. Upon adjustment to pH 7.0, the fibrils changed into amorphous aggregates, accompanied by a structural transition to random coils. Pretreatment of MBP with neutral protease and chymotrypsin yielded hydrolysates with distinct peptide profiles, leading to the formation of fibrils with varied morphologies upon acidic heating. Furthermore, the antioxidant activity of MBP and its fibrillar aggregates was highly dependent on pH and structural state. While fibril formation at pH 2.0 led to a reduction in radical scavenging activity of MBP, the subsequent pH-shifted aggregates at pH 7.0 resulted in a significant enhancement of antioxidant capacity. These findings provide fundamental insights into the formation, stability, and bioactive properties of MBP fibrils, emphasizing their pH-dependent behavior. [ABSTRACT FROM AUTHOR] |
| Copyright of Antioxidants is the property of MDPI and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Βάση Δεδομένων: | Complementary Index |
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| Items | – Name: Title Label: Title Group: Ti Data: Effect of pH on the Formation, Disintegration and Antioxidant Activity of Mung Bean Protein Fibrils. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Tian%2C+Yike%22">Tian, Yike</searchLink><br /><searchLink fieldCode="AR" term="%22Zhang%2C+Shuning%22">Zhang, Shuning</searchLink><br /><searchLink fieldCode="AR" term="%22Huang%2C+Weining%22">Huang, Weining</searchLink><br /><searchLink fieldCode="AR" term="%22Li%2C+Ning%22">Li, Ning</searchLink><br /><searchLink fieldCode="AR" term="%22Liang%2C+Li%22">Liang, Li</searchLink> – Name: TitleSource Label: Source Group: Src Data: Antioxidants; Dec2025, Vol. 14 Issue 12, p1399, 15p – Name: Subject Label: Subject Terms Group: Su Data: <searchLink fieldCode="DE" term="%22Hydrogen-ion+concentration%22">Hydrogen-ion concentration</searchLink><br /><searchLink fieldCode="DE" term="%22Antioxidants%22">Antioxidants</searchLink><br /><searchLink fieldCode="DE" term="%22Protein+structure%22">Protein structure</searchLink><br /><searchLink fieldCode="DE" term="%22Bioactive+compounds%22">Bioactive compounds</searchLink><br /><searchLink fieldCode="DE" term="%22Plant+proteins%22">Plant proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Peptides%22">Peptides</searchLink><br /><searchLink fieldCode="DE" term="%22Microfibrils%22">Microfibrils</searchLink><br /><searchLink fieldCode="DE" term="%22Hydrolysis%22">Hydrolysis</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Protein fibrils are highly ordered structures. Mung bean protein (MBP) fibrils were fabricated after heating under acidic condition. The formation mechanism, structural variety and antioxidant capacities of mung bean protein fibrils were investigated under different pH conditions. The fibrillation process was characterized by extensive hydrolysis of MBP into low-molecular-weight peptides, which subsequently self-assembled into fibrils with increasing contour length over time. The formed fibrils exhibited a dominant β-sheet structure but demonstrated high sensitivity to pH changes. Upon adjustment to pH 7.0, the fibrils changed into amorphous aggregates, accompanied by a structural transition to random coils. Pretreatment of MBP with neutral protease and chymotrypsin yielded hydrolysates with distinct peptide profiles, leading to the formation of fibrils with varied morphologies upon acidic heating. Furthermore, the antioxidant activity of MBP and its fibrillar aggregates was highly dependent on pH and structural state. While fibril formation at pH 2.0 led to a reduction in radical scavenging activity of MBP, the subsequent pH-shifted aggregates at pH 7.0 resulted in a significant enhancement of antioxidant capacity. These findings provide fundamental insights into the formation, stability, and bioactive properties of MBP fibrils, emphasizing their pH-dependent behavior. [ABSTRACT FROM AUTHOR] – Name: Abstract Label: Group: Ab Data: <i>Copyright of Antioxidants is the property of MDPI and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.3390/antiox14121399 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 15 StartPage: 1399 Subjects: – SubjectFull: Hydrogen-ion concentration Type: general – SubjectFull: Antioxidants Type: general – SubjectFull: Protein structure Type: general – SubjectFull: Bioactive compounds Type: general – SubjectFull: Plant proteins Type: general – SubjectFull: Peptides Type: general – SubjectFull: Microfibrils Type: general – SubjectFull: Hydrolysis Type: general Titles: – TitleFull: Effect of pH on the Formation, Disintegration and Antioxidant Activity of Mung Bean Protein Fibrils. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Tian, Yike – PersonEntity: Name: NameFull: Zhang, Shuning – PersonEntity: Name: NameFull: Huang, Weining – PersonEntity: Name: NameFull: Li, Ning – PersonEntity: Name: NameFull: Liang, Li IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 12 Text: Dec2025 Type: published Y: 2025 Identifiers: – Type: issn-print Value: 20763921 Numbering: – Type: volume Value: 14 – Type: issue Value: 12 Titles: – TitleFull: Antioxidants Type: main |
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