Latex peptidases produce peptides capable of delaying fungal growth in bread
Autor: | João P.B. Oliveira, Rafael Audino Zambelli, Pedro F.N. Souza, Jefferson Soares de Oliveira, Deborah C. Freitas, Márcio V. Ramos, Cleverson D.T. Freitas, Ayrles F.B. Silva, Leandro P. Bezerra, Glauber Batista Moreira Santos, Celso Shiniti Nagano |
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Rok vydání: | 2022 |
Předmět: |
Latex
biology Chemistry Aspergillus niger Antimicrobial peptides food and beverages Bread General Medicine biology.organism_classification Trypsin Analytical Chemistry Calotropis Calotropis procera Penicillium medicine Food science Carica Peptides Pythium oligandrum Antimicrobial Peptides Trichoderma reesei Peptide Hydrolases Food Science medicine.drug |
Zdroj: | Food Chemistry. 373:131410 |
ISSN: | 0308-8146 |
DOI: | 10.1016/j.foodchem.2021.131410 |
Popis: | Antimicrobial peptides (AMPs) have been reported to be promising alternatives to chemical preservatives. Thus, this study aimed to characterise AMPs generated from the hydrolysis of wheat gluten proteins using latex peptidases of Calotropis procera, Cryptostegia grandiflora, and Carica papaya. The three hydrolysates (obtained after 16 h at 37 °C, using a 1: 25 enzyme: substrate ratio) inhibited the growth of Aspergillus niger, A. chevalieri, Trichoderma reesei, Pythium oligandrum, Penicillium sp., and Lasiodiplodia sp. by 60-90%, and delayed fungal growth on bread by 3 days when used at 0.3 g/kg. Moreover, the specific volume and expansion factor of bread were not affected by the hydrolysates. Of 28 peptides identified, four were synthesised and exhibited activity against Penicillium sp. Fluorescence and scanning electron microscopy suggested that the peptides damaged the fungal plasma membrane. Bioinformatics analysis showed that no peptide was toxic and that the antigenic ones had cleavage sites for trypsin or pepsin. |
Databáze: | OpenAIRE |
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