Purification of protease from Coriandrum sativum using ion-exchange chromatography and gel filtration method

Authors

  • Baskaran Gunasekaran Department of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, University Putra Malaysia, UPM 43400 Serdang, Selangor, Malaysia
  • M.A. Syed Department of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, University Putra Malaysia, UPM 43400 Serdang, Selangor, Malaysia
  • Shamala Salvamani Department of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, University Putra Malaysia, UPM 43400 Serdang, Selangor, Malaysia
  • Subathra Sinniah Department of Chemistry, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia
  • Parveen Devi Pattiram Department of Food Technology, Faculty of Food Science and Technology, Universiti Putra Malaysia, 43400 UPM Serdang Selangor, Malaysia
  • Mohd Khalizan Sabullah Department of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, University Putra Malaysia, UPM 43400 Serdang, Selangor, Malaysia
  • Mohd Yunus Shukor Department of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, University Putra Malaysia, UPM 43400 Serdang, Selangor, Malaysia

DOI:

https://doi.org/10.54987/bessm.v2i2.197

Keywords:

plant protease, Coriandrum sativum, anion exchanger, gel filtration

Abstract

In the past decades, the interest towards plant proteases has increased significantly. Plant proteases are widely used in environment field, food and medicine industries. Proteases such as bromelain, papain and ficin are used in various areas such as in biosensors for detection of heavy metals, meat tenderization, brewing, cancer treatment, milk-clotting, viral disorders and digestion. In this study, protease from coriander leaf (Coriandrum sativum) was evaluated for protease activity using a Bradford-protease-casein assay system.  This enzyme was purified through anion exchanger using DEAE-Cellulose column and gel filtration using Agilent ZORBAX column. Its molecular weight was around 55 kDa. The specific activity of the purified protein is 45.0 units/mg protein, total activity is 2745.0 units, yield 33.2% and fold purification is 2.8. Further investigation on gene sequence should be performed in order to identify the type of protease involved.

Published

2014-12-03

How to Cite

Gunasekaran, B., Syed, M., Salvamani, S., Sinniah, S., Pattiram, P. D., Sabullah, M. K., & Shukor, M. Y. (2014). Purification of protease from Coriandrum sativum using ion-exchange chromatography and gel filtration method. Bulletin of Environmental Science and Sustainable Management (e-ISSN 2716-5353), 2(2), 53–57. https://doi.org/10.54987/bessm.v2i2.197

Issue

Vol. 2 No. 2 (2014)

Section

Articles

License

Authors who publish with this journal agree to the following terms:

  1. Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0) that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.
  2. Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgement of its initial publication in this journal.
  3. Authors are permitted and encouraged to post their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work (See The Effect of Open Access).