Protease purification from Bacillus amyloliquefaciens B7 using aqueous two phase system

Bacillus amyloliquefaciens B7 was isolated from fish fermented sauce and identified as protease producer. Generally, in downstream processing, purification of enzyme consumes high cost in terms of reagents and equipment used. Moreover, harsh purification methods used might cause denaturation of en...

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Main Authors:	Abd Samad , Nadiah Syuhada, Amid, Azura, Jimat, Dzun Noraini, Ab. Shukor, Nurul Aqilah
Format:	Conference or Workshop Item
Language:	English
Published:	Kulliyah of Engineering, International Islamic University Malaysia 2016
Subjects:	Q Science (General)
Online Access:	http://irep.iium.edu.my/51790/ http://irep.iium.edu.my/51790/ http://irep.iium.edu.my/51790/1/51790.pdf

id	iium-51790
recordtype	eprints
spelling	iium-517902016-08-24T07:37:13Z http://irep.iium.edu.my/51790/ Protease purification from Bacillus amyloliquefaciens B7 using aqueous two phase system Abd Samad , Nadiah Syuhada Amid, Azura Jimat, Dzun Noraini Ab. Shukor, Nurul Aqilah Q Science (General) Bacillus amyloliquefaciens B7 was isolated from fish fermented sauce and identified as protease producer. Generally, in downstream processing, purification of enzyme consumes high cost in terms of reagents and equipment used. Moreover, harsh purification methods used might cause denaturation of enzymes. Therefore, there is a high demand for efficient and low-cost extraction and purification methods. Aqueous two-phase system (ATPS) is an alternative that should be considered as it is simple, rapid separation yet cause little denaturation. Protease produced by B. amyloliquefaciens B7 was partitioned in two different ATPS, which are PEG/potassium phosphate and PEG/sodium citrate, and best separation was found in PEG/sodium citrate based on protease specific activity. Protease activity was determined using casein as the substrate. Using response surface methodology design, two independent variables which are pH and temperature were varied during protease purification by aqueous two-phase system composed of PEG 1500/sodium citrate and the highest enzyme activity was found at the interface phase. Optimum purification method observed is at pH 6, 30OC, 27 % (w/w) of PEG and 34 % (w/w) of Sodium Citrate and the highest enzyme activity achieved is 0.19± 0.010 U/ml. Kulliyah of Engineering, International Islamic University Malaysia 2016 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/51790/1/51790.pdf Abd Samad , Nadiah Syuhada and Amid, Azura and Jimat, Dzun Noraini and Ab. Shukor, Nurul Aqilah (2016) Protease purification from Bacillus amyloliquefaciens B7 using aqueous two phase system. In: 4th International Conference on Biotechnology Engineering 2016 (ICBioE 2016), 25th-27th July 2016, Kuala Lumpur. http://www.iium.edu.my/icbioe/2016/
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	Q Science (General)
spellingShingle	Q Science (General) Abd Samad , Nadiah Syuhada Amid, Azura Jimat, Dzun Noraini Ab. Shukor, Nurul Aqilah Protease purification from Bacillus amyloliquefaciens B7 using aqueous two phase system
description	Bacillus amyloliquefaciens B7 was isolated from fish fermented sauce and identified as protease producer. Generally, in downstream processing, purification of enzyme consumes high cost in terms of reagents and equipment used. Moreover, harsh purification methods used might cause denaturation of enzymes. Therefore, there is a high demand for efficient and low-cost extraction and purification methods. Aqueous two-phase system (ATPS) is an alternative that should be considered as it is simple, rapid separation yet cause little denaturation. Protease produced by B. amyloliquefaciens B7 was partitioned in two different ATPS, which are PEG/potassium phosphate and PEG/sodium citrate, and best separation was found in PEG/sodium citrate based on protease specific activity. Protease activity was determined using casein as the substrate. Using response surface methodology design, two independent variables which are pH and temperature were varied during protease purification by aqueous two-phase system composed of PEG 1500/sodium citrate and the highest enzyme activity was found at the interface phase. Optimum purification method observed is at pH 6, 30OC, 27 % (w/w) of PEG and 34 % (w/w) of Sodium Citrate and the highest enzyme activity achieved is 0.19± 0.010 U/ml.
format	Conference or Workshop Item
author	Abd Samad , Nadiah Syuhada Amid, Azura Jimat, Dzun Noraini Ab. Shukor, Nurul Aqilah
author_facet	Abd Samad , Nadiah Syuhada Amid, Azura Jimat, Dzun Noraini Ab. Shukor, Nurul Aqilah
author_sort	Abd Samad , Nadiah Syuhada
title	Protease purification from Bacillus amyloliquefaciens B7 using aqueous two phase system
title_short	Protease purification from Bacillus amyloliquefaciens B7 using aqueous two phase system
title_full	Protease purification from Bacillus amyloliquefaciens B7 using aqueous two phase system
title_fullStr	Protease purification from Bacillus amyloliquefaciens B7 using aqueous two phase system
title_full_unstemmed	Protease purification from Bacillus amyloliquefaciens B7 using aqueous two phase system
title_sort	protease purification from bacillus amyloliquefaciens b7 using aqueous two phase system
publisher	Kulliyah of Engineering, International Islamic University Malaysia
publishDate	2016
url	http://irep.iium.edu.my/51790/ http://irep.iium.edu.my/51790/ http://irep.iium.edu.my/51790/1/51790.pdf
first_indexed	2023-09-18T21:13:25Z
last_indexed	2023-09-18T21:13:25Z
_version_	1777411403818205184

Protease purification from Bacillus amyloliquefaciens B7 using aqueous two phase system

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