Academic Journal
Controlled hydrolysis and EGCG conjugation enhance the ADH/ALDH activation activity of chia seed meal protein hydrolysates: Fabrication and structural characterization.
| Τίτλος: | Controlled hydrolysis and EGCG conjugation enhance the ADH/ALDH activation activity of chia seed meal protein hydrolysates: Fabrication and structural characterization. |
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| Συγγραφείς: | Chen J; State Key Laboratory of Food Science and Resource, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China., Ge W; State Key Laboratory of Food Science and Resource, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China., Wang Y; State Key Laboratory of Food Science and Resource, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China., Hu Z; State Key Laboratory of Food Science and Resource, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China., Lv W; State Key Laboratory of Food Science and Resource, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China., Ma C; State Key Laboratory of Food Science and Resource, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China. Electronic address: machaoyang24@jiangnan.edu.cn., Wang H; State Key Laboratory of Food Science and Resource, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China. Electronic address: hxwang@jiangnan.edu.cn. |
| Πηγή: | Food chemistry [Food Chem] 2025 Jun 01; Vol. 476, pp. 143386. Date of Electronic Publication: 2025 Feb 11. |
| Τύπος έκδοσης: | Journal Article |
| Γλώσσα: | English |
| Στοιχεία περιοδικού: | Publisher: Elsevier Applied Science Publishers Country of Publication: England NLM ID: 7702639 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-7072 (Electronic) Linking ISSN: 03088146 NLM ISO Abbreviation: Food Chem Subsets: MEDLINE |
| Imprint Name(s): | Publication: Barking : Elsevier Applied Science Publishers Original Publication: Barking, Eng., Applied Science Publishers. |
| Ιατρικοί όροι (MeSH): | Protein Hydrolysates*/chemistry , Catechin*/chemistry , Catechin*/analogs & derivatives , Plant Proteins*/chemistry , Alcohol Dehydrogenase*/chemistry , Alcohol Dehydrogenase*/metabolism , Aldehyde Dehydrogenase*/chemistry , Aldehyde Dehydrogenase*/metabolism , Salvia*/chemistry, Seeds/chemistry ; Hydrolysis ; Enzyme Activation ; Molecular Docking Simulation ; Plant Extracts ; Salvia hispanica |
| Περίληψη: | This study examines the effects of hydrolysis duration (20-100 min using flavourzyme) and EGCG conjugation on the structure and bioactivity of chia seed meal protein hydrolysates (CSPH) through multi-spectroscopic techniques and physicochemical property evaluation. Subsequently, the activation effects of EGCG-conjugated peptides on alcohol metabolism-related enzymes were further analyzed through the integration of peptidomics, bioinformatics, and computational chemistry. It was found that with the extension of hydrolysis time, the thermal stability of CSPH diminishes, its rigid structure becomes more flexible, and its crystallinity decreases (by up to 27.19 %). Meanwhile, the activation effects on alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) activity were significantly enhanced (P < 0.05). CSPH hydrolyzed for 60 min demonstrated the highest binding affinity for EGCG, primarily driven by hydrophobic interactions and hydrogen bonds. The CSPH-EGCG conjugate exhibited enhanced physicochemical properties and significantly elevated activation of ADH and ALDH, with ADH activation rising from 22.66 % to 95.56 % and ALDH activation from 9.45 % to 30.93 %, compared to unmodified CSPH. Seven active peptides were identified from PE-60 by peptidomics and bioinformatics. Computer docking optimized selected three optimal peptides (IPW, FPIH, and IYP). Two-dimensional and three-dimensional interaction analyses showed that these peptides bind to EGCG, ADH, and ALDH via hydrogen bonds, hydrophobic interactions, and salt bridges. These findings highlight the potential of controlled hydrolysis with flavourzyme and EGCG incorporation to enhance CSPH's properties and bioactivities and offer insights into the practical applications of CSPH and its EGCG complexes in food processing and therapeutic systems. (Copyright © 2025 Elsevier Ltd. All rights reserved.) |
| Competing Interests: | Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. |
| Contributed Indexing: | Keywords: ADH/ALDH activation; Chia seed meal protein hydrolysate; Computational chemistry; Conjugate; EGCG |
| Substance Nomenclature: | 0 (Protein Hydrolysates) 8R1V1STN48 (Catechin) BQM438CTEL (epigallocatechin gallate) 0 (Plant Proteins) EC 1.1.1.1 (Alcohol Dehydrogenase) EC 1.2.1.3 (Aldehyde Dehydrogenase) 0 (Salvia hispanica seed extract) 0 (Plant Extracts) |
| Entry Date(s): | Date Created: 20250220 Date Completed: 20250509 Latest Revision: 20260127 |
| Update Code: | 20260130 |
| DOI: | 10.1016/j.foodchem.2025.143386 |
| PMID: | 39977998 |
| Βάση Δεδομένων: | MEDLINE |
| ISSN: | 1873-7072 |
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| DOI: | 10.1016/j.foodchem.2025.143386 |