Screening, Purification and Characterization of Protease Inhibitor from Capsicum frutescens

Plants are rich in protease inhibitors (PI) and trypsin inhibitors are the most common. Therefore, it is of interest to screen PI from plant sources. We report the screening, purification and characterization of PI from Capsicum frutescenes. The partially purified PI showed bands corresponding to 21...

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Autores principales: Mohan, Manju, Kozhithodi, Shireen, Nayarisseri, Anuraj, Elyas, Kothanam Kuzhiyil
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2018
Materias:
Hypothesis
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6137568/
https://www.ncbi.nlm.nih.gov/pubmed/30237674
http://dx.doi.org/10.6026/97320630014285
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author Mohan, Manju
Kozhithodi, Shireen
Nayarisseri, Anuraj
Elyas, Kothanam Kuzhiyil
author_facet Mohan, Manju
Kozhithodi, Shireen
Nayarisseri, Anuraj
Elyas, Kothanam Kuzhiyil
author_sort Mohan, Manju
collection PubMed
description Plants are rich in protease inhibitors (PI) and trypsin inhibitors are the most common. Therefore, it is of interest to screen PI from plant sources. We report the screening, purification and characterization of PI from Capsicum frutescenes. The partially purified PI showed bands corresponding to 21 KDa and was further confirmed using reverse zymography. The enzyme was stable at temperatures below 60°C and a wide range of pH with 65 folds purification. The effect of magnesium ions oxidizing and reducing agents on PI is reported. The large-scale isolation and purification of PI from Capsicum frutescenes is of commercial interest.
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spelling pubmed-61375682018-09-20 Screening, Purification and Characterization of Protease Inhibitor from Capsicum frutescens Mohan, Manju Kozhithodi, Shireen Nayarisseri, Anuraj Elyas, Kothanam Kuzhiyil Bioinformation Hypothesis Plants are rich in protease inhibitors (PI) and trypsin inhibitors are the most common. Therefore, it is of interest to screen PI from plant sources. We report the screening, purification and characterization of PI from Capsicum frutescenes. The partially purified PI showed bands corresponding to 21 KDa and was further confirmed using reverse zymography. The enzyme was stable at temperatures below 60°C and a wide range of pH with 65 folds purification. The effect of magnesium ions oxidizing and reducing agents on PI is reported. The large-scale isolation and purification of PI from Capsicum frutescenes is of commercial interest. Biomedical Informatics 2018-06-30 /pmc/articles/PMC6137568/ /pubmed/30237674 http://dx.doi.org/10.6026/97320630014285 Text en © 2018 Biomedical Informatics http://creativecommons.org/licenses/by/3.0/ This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.
spellingShingle Hypothesis
Mohan, Manju
Kozhithodi, Shireen
Nayarisseri, Anuraj
Elyas, Kothanam Kuzhiyil
Screening, Purification and Characterization of Protease Inhibitor from Capsicum frutescens
title Screening, Purification and Characterization of Protease Inhibitor from Capsicum frutescens
title_full Screening, Purification and Characterization of Protease Inhibitor from Capsicum frutescens
title_fullStr Screening, Purification and Characterization of Protease Inhibitor from Capsicum frutescens
title_full_unstemmed Screening, Purification and Characterization of Protease Inhibitor from Capsicum frutescens
title_short Screening, Purification and Characterization of Protease Inhibitor from Capsicum frutescens
title_sort screening, purification and characterization of protease inhibitor from capsicum frutescens
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6137568/
https://www.ncbi.nlm.nih.gov/pubmed/30237674
http://dx.doi.org/10.6026/97320630014285
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