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Biotechnological Potential of Araucaria angustifolia Pine Nuts Extract and the Cysteine Protease Inhibitor AaCI-2S
Protease inhibitors are involved in the regulation of endogenous cysteine proteases during seed development and play a defensive role because of their ability to inhibit exogenous proteases such as those present in the digestive tracts of insects. Araucaria angustifolia seeds, which can be used in h...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7760129/ https://www.ncbi.nlm.nih.gov/pubmed/33266031 http://dx.doi.org/10.3390/plants9121676 |
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author | Sallai, Roberto Carlos Salu, Bruno Ramos Silva-Lucca, Rosemeire Aparecida Alves, Flávio Lopes Napoleão, Thiago Henrique Paiva, Patrícia Maria Guedes da Silva Ferreira, Rodrigo Sampaio, Misako Uemura Vilela Oliva, Maria Luiza |
author_facet | Sallai, Roberto Carlos Salu, Bruno Ramos Silva-Lucca, Rosemeire Aparecida Alves, Flávio Lopes Napoleão, Thiago Henrique Paiva, Patrícia Maria Guedes da Silva Ferreira, Rodrigo Sampaio, Misako Uemura Vilela Oliva, Maria Luiza |
author_sort | Sallai, Roberto Carlos |
collection | PubMed |
description | Protease inhibitors are involved in the regulation of endogenous cysteine proteases during seed development and play a defensive role because of their ability to inhibit exogenous proteases such as those present in the digestive tracts of insects. Araucaria angustifolia seeds, which can be used in human and animal feed, were investigated for their potential for the development of agricultural biotechnology and in the field of human health. In the pine nuts extract, which blocked the activities of cysteine proteases, it was detected potent insecticidal activity against termites (Nasutitermes corniger) belonging to the most abundant termite genus in tropical regions. The cysteine inhibitor (AaCI-2S) was purified by ion-exchange, size exclusion, and reversed-phase chromatography. Its functional and structural stability was confirmed by spectroscopic and circular dichroism studies, and by detection of inhibitory activity at different temperatures and pH values. Besides having activity on cysteine proteases from C. maculatus digestive tract, AaCI-2S inhibited papain, bromelain, ficin, and cathepsin L and impaired cell proliferation in gastric and prostate cancer cell lines. These properties qualify A. angustifolia seeds as a protein source with value properties of natural insecticide and to contain a protease inhibitor with the potential to be a bioactive molecule on different cancer cells. |
format | Online Article Text |
id | pubmed-7760129 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-77601292020-12-26 Biotechnological Potential of Araucaria angustifolia Pine Nuts Extract and the Cysteine Protease Inhibitor AaCI-2S Sallai, Roberto Carlos Salu, Bruno Ramos Silva-Lucca, Rosemeire Aparecida Alves, Flávio Lopes Napoleão, Thiago Henrique Paiva, Patrícia Maria Guedes da Silva Ferreira, Rodrigo Sampaio, Misako Uemura Vilela Oliva, Maria Luiza Plants (Basel) Article Protease inhibitors are involved in the regulation of endogenous cysteine proteases during seed development and play a defensive role because of their ability to inhibit exogenous proteases such as those present in the digestive tracts of insects. Araucaria angustifolia seeds, which can be used in human and animal feed, were investigated for their potential for the development of agricultural biotechnology and in the field of human health. In the pine nuts extract, which blocked the activities of cysteine proteases, it was detected potent insecticidal activity against termites (Nasutitermes corniger) belonging to the most abundant termite genus in tropical regions. The cysteine inhibitor (AaCI-2S) was purified by ion-exchange, size exclusion, and reversed-phase chromatography. Its functional and structural stability was confirmed by spectroscopic and circular dichroism studies, and by detection of inhibitory activity at different temperatures and pH values. Besides having activity on cysteine proteases from C. maculatus digestive tract, AaCI-2S inhibited papain, bromelain, ficin, and cathepsin L and impaired cell proliferation in gastric and prostate cancer cell lines. These properties qualify A. angustifolia seeds as a protein source with value properties of natural insecticide and to contain a protease inhibitor with the potential to be a bioactive molecule on different cancer cells. MDPI 2020-11-30 /pmc/articles/PMC7760129/ /pubmed/33266031 http://dx.doi.org/10.3390/plants9121676 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Sallai, Roberto Carlos Salu, Bruno Ramos Silva-Lucca, Rosemeire Aparecida Alves, Flávio Lopes Napoleão, Thiago Henrique Paiva, Patrícia Maria Guedes da Silva Ferreira, Rodrigo Sampaio, Misako Uemura Vilela Oliva, Maria Luiza Biotechnological Potential of Araucaria angustifolia Pine Nuts Extract and the Cysteine Protease Inhibitor AaCI-2S |
title | Biotechnological Potential of Araucaria angustifolia Pine Nuts Extract and the Cysteine Protease Inhibitor AaCI-2S |
title_full | Biotechnological Potential of Araucaria angustifolia Pine Nuts Extract and the Cysteine Protease Inhibitor AaCI-2S |
title_fullStr | Biotechnological Potential of Araucaria angustifolia Pine Nuts Extract and the Cysteine Protease Inhibitor AaCI-2S |
title_full_unstemmed | Biotechnological Potential of Araucaria angustifolia Pine Nuts Extract and the Cysteine Protease Inhibitor AaCI-2S |
title_short | Biotechnological Potential of Araucaria angustifolia Pine Nuts Extract and the Cysteine Protease Inhibitor AaCI-2S |
title_sort | biotechnological potential of araucaria angustifolia pine nuts extract and the cysteine protease inhibitor aaci-2s |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7760129/ https://www.ncbi.nlm.nih.gov/pubmed/33266031 http://dx.doi.org/10.3390/plants9121676 |
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