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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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Title: Controlled hydrolysis and EGCG conjugation enhance the ADH/ALDH activation activity of chia seed meal protein hydrolysates: Fabrication and structural characterization.
Authors: 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.
Source: Food chemistry [Food Chem] 2025 Jun 01; Vol. 476, pp. 143386. Date of Electronic Publication: 2025 Feb 11.
Publication Type: Journal Article
Language: English
Journal Info: 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.
MeSH Terms: 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
Abstract: 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
Database: MEDLINE
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  Label: Title
  Group: Ti
  Data: 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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  Label: Authors
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  Data: &lt;searchLink fieldCode=&quot;AU&quot; term=&quot;%22Chen+J%22&quot;&gt;Chen J&lt;/searchLink&gt;; State Key Laboratory of Food Science and Resource, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.&lt;br /&gt;&lt;searchLink fieldCode=&quot;AU&quot; term=&quot;%22Ge+W%22&quot;&gt;Ge W&lt;/searchLink&gt;; State Key Laboratory of Food Science and Resource, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.&lt;br /&gt;&lt;searchLink fieldCode=&quot;AU&quot; term=&quot;%22Wang+Y%22&quot;&gt;Wang Y&lt;/searchLink&gt;; State Key Laboratory of Food Science and Resource, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.&lt;br /&gt;&lt;searchLink fieldCode=&quot;AU&quot; term=&quot;%22Hu+Z%22&quot;&gt;Hu Z&lt;/searchLink&gt;; State Key Laboratory of Food Science and Resource, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.&lt;br /&gt;&lt;searchLink fieldCode=&quot;AU&quot; term=&quot;%22Lv+W%22&quot;&gt;Lv W&lt;/searchLink&gt;; State Key Laboratory of Food Science and Resource, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.&lt;br /&gt;&lt;searchLink fieldCode=&quot;AU&quot; term=&quot;%22Ma+C%22&quot;&gt;Ma C&lt;/searchLink&gt;; 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.&lt;br /&gt;&lt;searchLink fieldCode=&quot;AU&quot; term=&quot;%22Wang+H%22&quot;&gt;Wang H&lt;/searchLink&gt;; 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.
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  Data: &lt;searchLink fieldCode=&quot;JN&quot; term=&quot;%227702639%22&quot;&gt;Food chemistry&lt;/searchLink&gt; [Food Chem] 2025 Jun 01; Vol. 476, pp. 143386. &lt;i&gt;Date of Electronic Publication: &lt;/i&gt;2025 Feb 11.
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  Data: &lt;i&gt;Publication&lt;/i&gt;: Barking : Elsevier Applied Science Publishers&lt;br /&gt;&lt;i&gt;Original Publication&lt;/i&gt;: Barking, Eng., Applied Science Publishers.
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  Data: &lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Protein+Hydrolysates%22&quot;&gt;Protein Hydrolysates*&lt;/searchLink&gt;/&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Protein+Hydrolysates+chemistry%22&quot;&gt;chemistry&lt;/searchLink&gt; &lt;br /&gt;&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Catechin%22&quot;&gt;Catechin*&lt;/searchLink&gt;/&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Catechin+chemistry%22&quot;&gt;chemistry&lt;/searchLink&gt; &lt;br /&gt;&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Catechin%22&quot;&gt;Catechin*&lt;/searchLink&gt;/&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Catechin+analogs+%26+derivatives%22&quot;&gt;analogs &amp; derivatives&lt;/searchLink&gt; &lt;br /&gt;&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Plant+Proteins%22&quot;&gt;Plant Proteins*&lt;/searchLink&gt;/&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Plant+Proteins+chemistry%22&quot;&gt;chemistry&lt;/searchLink&gt; &lt;br /&gt;&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Alcohol+Dehydrogenase%22&quot;&gt;Alcohol Dehydrogenase*&lt;/searchLink&gt;/&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Alcohol+Dehydrogenase+chemistry%22&quot;&gt;chemistry&lt;/searchLink&gt; &lt;br /&gt;&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Alcohol+Dehydrogenase%22&quot;&gt;Alcohol Dehydrogenase*&lt;/searchLink&gt;/&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Alcohol+Dehydrogenase+metabolism%22&quot;&gt;metabolism&lt;/searchLink&gt; &lt;br /&gt;&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Aldehyde+Dehydrogenase%22&quot;&gt;Aldehyde Dehydrogenase*&lt;/searchLink&gt;/&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Aldehyde+Dehydrogenase+chemistry%22&quot;&gt;chemistry&lt;/searchLink&gt; &lt;br /&gt;&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Aldehyde+Dehydrogenase%22&quot;&gt;Aldehyde Dehydrogenase*&lt;/searchLink&gt;/&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Aldehyde+Dehydrogenase+metabolism%22&quot;&gt;metabolism&lt;/searchLink&gt; &lt;br /&gt;&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Salvia%22&quot;&gt;Salvia*&lt;/searchLink&gt;/&lt;searchLink fieldCode=&quot;MM&quot; term=&quot;%22Salvia+chemistry%22&quot;&gt;chemistry&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;MH&quot; term=&quot;%22Seeds%22&quot;&gt;Seeds&lt;/searchLink&gt;/&lt;searchLink fieldCode=&quot;MH&quot; term=&quot;%22Seeds+chemistry%22&quot;&gt;chemistry&lt;/searchLink&gt; ; &lt;searchLink fieldCode=&quot;MH&quot; term=&quot;%22Hydrolysis%22&quot;&gt;Hydrolysis&lt;/searchLink&gt; ; &lt;searchLink fieldCode=&quot;MH&quot; term=&quot;%22Enzyme+Activation%22&quot;&gt;Enzyme Activation&lt;/searchLink&gt; ; &lt;searchLink fieldCode=&quot;MH&quot; term=&quot;%22Molecular+Docking+Simulation%22&quot;&gt;Molecular Docking Simulation&lt;/searchLink&gt; ; &lt;searchLink fieldCode=&quot;MH&quot; term=&quot;%22Plant+Extracts%22&quot;&gt;Plant Extracts&lt;/searchLink&gt; ; &lt;searchLink fieldCode=&quot;MH&quot; term=&quot;%22Salvia+hispanica%22&quot;&gt;Salvia hispanica&lt;/searchLink&gt;
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: This study examines the effects of hydrolysis duration (20-100&#160;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&#160;%). Meanwhile, the activation effects on alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) activity were significantly enhanced (P&#160;&amp;lt;&#160;0.05). CSPH hydrolyzed for 60&#160;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&#160;% to 95.56&#160;% and ALDH activation from 9.45&#160;% to 30.93&#160;%, 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&#39;s properties and bioactivities and offer insights into the practical applications of CSPH and its EGCG complexes in food processing and therapeutic systems.&lt;br /&gt; (Copyright &#169; 2025 Elsevier Ltd. All rights reserved.)
– Name: Abstract
  Label: Competing Interests
  Group: Ab
  Data: 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.
– Name: SubjectMinor
  Label: Contributed Indexing
  Group:
  Data: &lt;i&gt;Keywords: &lt;/i&gt;ADH/ALDH activation; Chia seed meal protein hydrolysate; Computational chemistry; Conjugate; EGCG
– Name: NumberCAS
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  Data: 0 (Protein Hydrolysates)&lt;br /&gt;8R1V1STN48 (Catechin)&lt;br /&gt;BQM438CTEL (epigallocatechin gallate)&lt;br /&gt;0 (Plant Proteins)&lt;br /&gt;EC 1.1.1.1 (Alcohol Dehydrogenase)&lt;br /&gt;EC 1.2.1.3 (Aldehyde Dehydrogenase)&lt;br /&gt;0 (Salvia hispanica seed extract)&lt;br /&gt;0 (Plant Extracts)
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  Data: &lt;i&gt;Date Created: &lt;/i&gt;20250220 &lt;i&gt;Date Completed: &lt;/i&gt;20250509 &lt;i&gt;Latest Revision: &lt;/i&gt;20260127
– Name: DateUpdate
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  Data: 20260130
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  Data: 10.1016/j.foodchem.2025.143386
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  Data: 39977998
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=cmedm&AN=39977998
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        Value: 10.1016/j.foodchem.2025.143386
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      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        StartPage: 143386
    Subjects:
      – SubjectFull: Seeds chemistry
        Type: general
      – SubjectFull: Hydrolysis
        Type: general
      – SubjectFull: Enzyme Activation
        Type: general
      – SubjectFull: Molecular Docking Simulation
        Type: general
      – SubjectFull: Plant Extracts
        Type: general
      – SubjectFull: Salvia hispanica
        Type: general
      – SubjectFull: Protein Hydrolysates chemistry
        Type: general
      – SubjectFull: Catechin chemistry
        Type: general
      – SubjectFull: Catechin analogs & derivatives
        Type: general
      – SubjectFull: Plant Proteins chemistry
        Type: general
      – SubjectFull: Alcohol Dehydrogenase chemistry
        Type: general
      – SubjectFull: Alcohol Dehydrogenase metabolism
        Type: general
      – SubjectFull: Aldehyde Dehydrogenase chemistry
        Type: general
      – SubjectFull: Aldehyde Dehydrogenase metabolism
        Type: general
      – SubjectFull: Salvia chemistry
        Type: general
    Titles:
      – TitleFull: 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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            – D: 01
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              Text: 2025 Jun 01
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              Y: 2025
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