Characterization of New Protease from Murdannia Bracteata

Plant proteases occupy the most relevant position in the biotechnology and pharmaceutical industries due to their proteolytic activity on a wide range of temperature and pH. Plant protease such as papain, bromelain and ficin are the most frequently employed as industrial enzymes, although new protea...

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Main Authors:	N., Yahya, Zatul Iffah, Mohd Arshad, Rohaida, Che Man, Siti Kholijah, Abdul Mudalip, Siti Zubaidah, Sulaiman, Shalyda, Md Shaarani
Format:	Conference or Workshop Item
Language:	English
Published:	2018
Subjects:	TP Chemical technology
Online Access:	http://umpir.ump.edu.my/id/eprint/23645/ http://umpir.ump.edu.my/id/eprint/23645/1/Characterization%20of%20New%20Protease%20from%20Murdannia%20Bracteata.pdf

id	ump-23645
recordtype	eprints
spelling	ump-236452019-01-07T09:10:30Z http://umpir.ump.edu.my/id/eprint/23645/ Characterization of New Protease from Murdannia Bracteata N., Yahya Zatul Iffah, Mohd Arshad Rohaida, Che Man Siti Kholijah, Abdul Mudalip Siti Zubaidah, Sulaiman Shalyda, Md Shaarani TP Chemical technology Plant proteases occupy the most relevant position in the biotechnology and pharmaceutical industries due to their proteolytic activity on a wide range of temperature and pH. Plant protease such as papain, bromelain and ficin are the most frequently employed as industrial enzymes, although new proteases with more appealing physicochemical properties for industry are still emerging [1]. The Murdannia bracteata (C. B. Clarke) is an annual shrub that commonly found in Malaysia, China and Thailand. This plant has been claimed to exert antioxidant and hepatoprotective effect on rats [2]. However, the presence of protease in Murdannia bracteata plant have not been scientifically explored. Therefore, in the present study, screening of 7 different plant species for the optimum specific activity was investigated. The leaf extract from Murdannia bracteata showed relatively high specific activity that the protease extract from other plants. Therefore, the protease from the leaves of Murdannia bracteata was purified from the plant of Murdannia bracteata by ammonium sulfate precipitation at 10 % of saturation level. The purity of the protein was verified by SDS-PAGE analysis. Then, the characteristics of pH, temperature and inhibitors of purified protease from Murdannia bracteata extract were investigated. A single band of protease was visualised on SDS-PAGE with the molecular weight of 40 kDa. The protease had an optimum pH of 8.0 and was stable at 50°C with high specific activity. Complete inhibition of protease activity such as PMSF and EDTA indicates that the enzyme belongs to the serine protease class. Thus, protease from Murdannia bracteata might be a potential candidate for various applications in the food and biotechnological industries. 2018 Conference or Workshop Item PeerReviewed pdf en http://umpir.ump.edu.my/id/eprint/23645/1/Characterization%20of%20New%20Protease%20from%20Murdannia%20Bracteata.pdf N., Yahya and Zatul Iffah, Mohd Arshad and Rohaida, Che Man and Siti Kholijah, Abdul Mudalip and Siti Zubaidah, Sulaiman and Shalyda, Md Shaarani (2018) Characterization of New Protease from Murdannia Bracteata. In: 4th International Conference Of Chemical Engineering And Industrial Biotechnology (ICCEIB 2018), 1-2 Aug 2018 , Seri Pacific Hotel, Kuala Lumpur. p. 419..
repository_type	Digital Repository
institution_category	Local University
institution	Universiti Malaysia Pahang
building	UMP Institutional Repository
collection	Online Access
language	English
topic	TP Chemical technology
spellingShingle	TP Chemical technology N., Yahya Zatul Iffah, Mohd Arshad Rohaida, Che Man Siti Kholijah, Abdul Mudalip Siti Zubaidah, Sulaiman Shalyda, Md Shaarani Characterization of New Protease from Murdannia Bracteata
description	Plant proteases occupy the most relevant position in the biotechnology and pharmaceutical industries due to their proteolytic activity on a wide range of temperature and pH. Plant protease such as papain, bromelain and ficin are the most frequently employed as industrial enzymes, although new proteases with more appealing physicochemical properties for industry are still emerging [1]. The Murdannia bracteata (C. B. Clarke) is an annual shrub that commonly found in Malaysia, China and Thailand. This plant has been claimed to exert antioxidant and hepatoprotective effect on rats [2]. However, the presence of protease in Murdannia bracteata plant have not been scientifically explored. Therefore, in the present study, screening of 7 different plant species for the optimum specific activity was investigated. The leaf extract from Murdannia bracteata showed relatively high specific activity that the protease extract from other plants. Therefore, the protease from the leaves of Murdannia bracteata was purified from the plant of Murdannia bracteata by ammonium sulfate precipitation at 10 % of saturation level. The purity of the protein was verified by SDS-PAGE analysis. Then, the characteristics of pH, temperature and inhibitors of purified protease from Murdannia bracteata extract were investigated. A single band of protease was visualised on SDS-PAGE with the molecular weight of 40 kDa. The protease had an optimum pH of 8.0 and was stable at 50°C with high specific activity. Complete inhibition of protease activity such as PMSF and EDTA indicates that the enzyme belongs to the serine protease class. Thus, protease from Murdannia bracteata might be a potential candidate for various applications in the food and biotechnological industries.
format	Conference or Workshop Item
author	N., Yahya Zatul Iffah, Mohd Arshad Rohaida, Che Man Siti Kholijah, Abdul Mudalip Siti Zubaidah, Sulaiman Shalyda, Md Shaarani
author_facet	N., Yahya Zatul Iffah, Mohd Arshad Rohaida, Che Man Siti Kholijah, Abdul Mudalip Siti Zubaidah, Sulaiman Shalyda, Md Shaarani
author_sort	N., Yahya
title	Characterization of New Protease from Murdannia Bracteata
title_short	Characterization of New Protease from Murdannia Bracteata
title_full	Characterization of New Protease from Murdannia Bracteata
title_fullStr	Characterization of New Protease from Murdannia Bracteata
title_full_unstemmed	Characterization of New Protease from Murdannia Bracteata
title_sort	characterization of new protease from murdannia bracteata
publishDate	2018
url	http://umpir.ump.edu.my/id/eprint/23645/ http://umpir.ump.edu.my/id/eprint/23645/1/Characterization%20of%20New%20Protease%20from%20Murdannia%20Bracteata.pdf
first_indexed	2023-09-18T22:35:30Z
last_indexed	2023-09-18T22:35:30Z
_version_	1777416568549933056

Characterization of New Protease from Murdannia Bracteata

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