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Title

Screening, Purification and Characterization of Protease Inhibitor from Capsicum frutescens

 

Authors

Manju Mohan1, Shireen Kozhithodi1, Anuraj Nayarisseri2, Kothanam Kuzhiyil Elyas1*

 

Affiliation

1Department of Biotechnology, University of Calicut - 673635, Kerala, India;

2In silico Research Laboratory, Eminent Biosciences, Vijaynagar, Indore - 452010, Madhya Pradesh, India;

 

Email

kkelyas@yahoo.com;

 

Article Type

Hypothesis

 

Date

Received June 20, 2018; Revised June 25, 2018; Accepted June 27, 2018; Published June 30, 2018

 

Abstract

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 60C 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.

 

Keywords

Protease Inhibitor, Capsicum frutescens, purification, activity

 

Citation

Mohan et al. Bioinformation 14(6): 285-293 (2018)

 

Edited by

P Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

License

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.