A Study of the Interaction, Morphology, and Structure in Trypsin-Epigallocatechin-3-Gallate Complexes

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dc.citation.issue15
dc.citation.volume26
dc.contributor.authorLiu J
dc.contributor.authorGhanizadeh H
dc.contributor.authorLi X
dc.contributor.authorHan Z
dc.contributor.authorQiu Y
dc.contributor.authorZhang Y
dc.contributor.authorChen X
dc.contributor.authorWang A
dc.contributor.editorTresserra-Rimbau A
dc.contributor.editorBresciani L
dc.coverage.spatialSwitzerland
dc.date.accessioned2024-08-14T21:56:24Z
dc.date.available2024-08-14T21:56:24Z
dc.date.issued2021-07-28
dc.description.abstractUnderstanding the interaction between proteins and polyphenols is of significance to food industries. The aim of this research was to investigate the mode of aggregation for trypsin-EGCG (Epigallocatechin-3-gallate) complexes. For this, the complex was characterized by fluorescence spectroscopy, circular dichroism (CD) spectra, small-angel X-ray scattering (SAXS), and atomic force microscope (AFM) techniques. The results showed that the fluorescence intensity of trypsin-EGCG complexes decreased with increasing the concentration of EGCG, indicating that the interaction between trypsin and EGCG resulted in changes in the microenvironment around fluorescent amino acid residues. The results of CD analysis showed conformational changes in trypsin after binding with EGCG. The results from SAXS analysis showed that the addition of EGCG results in the formation of aggregates of trypsin-EGCG complexes, and increasing the concentration of EGCG resulted in larger aggregates. AFM images showed that the trypsin-EGCG complex formed aggregates of irregular ellipsoidal shapes with the size of about 200 × 400 × 200 nm, with EGCG interconnecting the trypsin particles. Overall, according to these results, it was concluded that the large aggregates of trypsin-EGCG complexes are formed from several small aggregates that are interconnected. The results of this study shed some light on the interaction between digestive enzymes and EGCG.
dc.description.confidentialfalse
dc.edition.editionAugust 2021
dc.format.pagination4567-
dc.identifier.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/34361715
dc.identifier.citationLiu J, Ghanizadeh H, Li X, Han Z, Qiu Y, Zhang Y, Chen X, Wang A. (2021). A Study of the Interaction, Morphology, and Structure in Trypsin-Epigallocatechin-3-Gallate Complexes.. Molecules. 26. 15. (pp. 4567-).
dc.identifier.doi10.3390/molecules26154567
dc.identifier.eissn1420-3049
dc.identifier.elements-typejournal-article
dc.identifier.issn1420-3049
dc.identifier.numberARTN 4567
dc.identifier.piimolecules26154567
dc.identifier.urihttps://mro.massey.ac.nz/handle/10179/71301
dc.languageeng
dc.publisherMDPI (Basel, Switzerland)
dc.publisher.urihttps://www.mdpi.com/1420-3049/26/15/4567
dc.relation.isPartOfMolecules
dc.rights(c) 2024 The Author/s
dc.rightsCC BY 4.0
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectEGCG
dc.subjectaggregates
dc.subjectpolyphenols
dc.subjectsmall-angel X-ray scattering
dc.subjecttrypsin
dc.subjectCatechin
dc.subjectHumans
dc.subjectMicroscopy, Atomic Force
dc.subjectModels, Molecular
dc.subjectProtein Aggregates
dc.subjectProtein Conformation
dc.subjectSolutions
dc.subjectSpectrometry, Fluorescence
dc.subjectTrypsin
dc.titleA Study of the Interaction, Morphology, and Structure in Trypsin-Epigallocatechin-3-Gallate Complexes
dc.typeJournal article
pubs.elements-id447965
pubs.organisational-groupOther
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