Article: The kiwifruit enzyme actinidin enhances the hydrolysis of gluten proteins during simulated gastrointestinal digestion
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. |
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| Keywords | bromelains ; epitopes ; food chemistry ; gastrointestinal system ; gliadin ; gluten ; hydrolysis ; in vitro digestion ; kiwifruit ; pH ; papain ; peptides ; proline |
| Language | English |
| Dates of publication | 2021-0330 |
| Publishing place | Elsevier Ltd |
| Document type | Article |
| Note | 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 |
| Database | NAL-Catalogue (AGRICOLA) |
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