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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Detalles Bibliográficos
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
Descripción
Sumario: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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