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  1. AU="McNabb, Warren C."
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  1. Artikel: The kiwifruit enzyme actinidin enhances the hydrolysis of gluten proteins during simulated gastrointestinal digestion

    Jayawardana, Isuri A / Boland, Mike J / Higgs, Keriane / Zou, Maggie / Loo, Trevor / Mcnabb, Warren C / Montoya, Carlos A

    Food chemistry. 2021 Mar. 30, v. 341

    2021  

    Abstract: This study investigated the effect of actinidin, a cysteine protease in kiwifruit, on the hydrolysis of gluten proteins and digestion-resistant gluten peptides (synthetic 33-mer peptide and pentapeptide epitopes) under static simulated gastrointestinal ... ...

    Abstract This study investigated the effect of actinidin, a cysteine protease in kiwifruit, on the hydrolysis of gluten proteins and digestion-resistant gluten peptides (synthetic 33-mer peptide and pentapeptide epitopes) under static simulated gastrointestinal conditions. Actinidin efficacy in hydrolysing gliadin was compared with that of other gluten-degrading enzymes. Actinidin hydrolysed usually resistant peptide bonds adjacent to proline residues in the 33-mer peptide. The gastric degree of hydrolysis of gluten proteins was influenced by an interaction between pH and actinidin concentration (P < 0.05), whereas the pentapeptide epitopes hydrolysis was influenced only by the actinidin concentration (P < 0.05). The rate of gastric degree of hydrolysis of gliadin was greater (P < 0.05) by actinidin (0.8%/min) when compared to papain, bromelain, and one commercial enzyme (on average 0.4%/min), while all exogenous enzymes were able to hydrolyse the pentapeptide epitopes effectively. Actinidin is able to hydrolyse gluten proteins under simulated gastric conditions.
    Schlagwörter bromelains ; epitopes ; food chemistry ; gastrointestinal system ; gliadin ; gluten ; hydrolysis ; in vitro digestion ; kiwifruit ; pH ; papain ; peptides ; proline
    Sprache Englisch
    Erscheinungsverlauf 2021-0330
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    Anmerkung NAL-light
    ZDB-ID 243123-3
    ISSN 1873-7072 ; 0308-8146
    ISSN (online) 1873-7072
    ISSN 0308-8146
    DOI 10.1016/j.foodchem.2020.128239
    Datenquelle NAL Katalog (AGRICOLA)

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  2. Artikel ; Online: The kiwifruit enzyme actinidin enhances the hydrolysis of gluten proteins during simulated gastrointestinal digestion.

    Jayawardana, Isuri A / Boland, Mike J / Higgs, Keriane / Zou, Maggie / Loo, Trevor / Mcnabb, Warren C / Montoya, Carlos A

    Food chemistry

    2020  Band 341, Heft Pt 1, Seite(n) 128239

    Abstract: This study investigated the effect of actinidin, a cysteine protease in kiwifruit, on the hydrolysis of gluten proteins and digestion-resistant gluten peptides (synthetic 33-mer peptide and pentapeptide epitopes) under static simulated gastrointestinal ... ...

    Abstract This study investigated the effect of actinidin, a cysteine protease in kiwifruit, on the hydrolysis of gluten proteins and digestion-resistant gluten peptides (synthetic 33-mer peptide and pentapeptide epitopes) under static simulated gastrointestinal conditions. Actinidin efficacy in hydrolysing gliadin was compared with that of other gluten-degrading enzymes. Actinidin hydrolysed usually resistant peptide bonds adjacent to proline residues in the 33-mer peptide. The gastric degree of hydrolysis of gluten proteins was influenced by an interaction between pH and actinidin concentration (P < 0.05), whereas the pentapeptide epitopes hydrolysis was influenced only by the actinidin concentration (P < 0.05). The rate of gastric degree of hydrolysis of gliadin was greater (P < 0.05) by actinidin (0.8%/min) when compared to papain, bromelain, and one commercial enzyme (on average 0.4%/min), while all exogenous enzymes were able to hydrolyse the pentapeptide epitopes effectively. Actinidin is able to hydrolyse gluten proteins under simulated gastric conditions.
    Mesh-Begriff(e) Actinidia/enzymology ; Biomimetics ; Cysteine Endopeptidases/metabolism ; Digestion ; Gastrointestinal Tract/physiology ; Glutens/metabolism ; Hydrolysis
    Chemische Substanzen Glutens (8002-80-0) ; Cysteine Endopeptidases (EC 3.4.22.-) ; actinidain (EC 3.4.22.14)
    Sprache Englisch
    Erscheinungsdatum 2020-10-01
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 243123-3
    ISSN 1873-7072 ; 0308-8146
    ISSN (online) 1873-7072
    ISSN 0308-8146
    DOI 10.1016/j.foodchem.2020.128239
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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