Title

Screening, Purification and Characterization of Protease Inhibitor from Capsicum frutescens

Authors

Manju Mohan¹, Shireen Kozhithodi¹, Anuraj Nayarisseri², Kothanam Kuzhiyil Elyas^1*

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

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.

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.