Purification of glutathione Transferases (GSTs) from identified Rhizospheric bacteria

The glutathione S-Transferase (GST) enzyme plays an important role in cellular detoxification. This multifunctional enzyme is involved in Phase II detoxification pathways that protect cellular macromolecules from being attacked by harmful compound. The study is an attempt to isolate glutathione tran...

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Main Authors:	Khanom Simarani, Wan Haizatul Akmal Che Yusoff, Zazali Alias
Format:	Article
Language:	English
Published:	Penerbit Universiti Kebangsaan Malaysia 2016
Online Access:	http://journalarticle.ukm.my/9979/ http://journalarticle.ukm.my/9979/ http://journalarticle.ukm.my/9979/1/07%20Khanom%20Simarani.pdf

id	ukm-9979
recordtype	eprints
spelling	ukm-99792017-01-19T09:22:48Z http://journalarticle.ukm.my/9979/ Purification of glutathione Transferases (GSTs) from identified Rhizospheric bacteria Khanom Simarani, Wan Haizatul Akmal Che Yusoff, Zazali Alias, The glutathione S-Transferase (GST) enzyme plays an important role in cellular detoxification. This multifunctional enzyme is involved in Phase II detoxification pathways that protect cellular macromolecules from being attacked by harmful compound. The study is an attempt to isolate glutathione transferase-expressing bacteria from the rhizospheric soil of selected herbal plants. Screening showed nine positive isolates out of twelve bacterial samples from a large microbial population in our soil collection. Crude extract from strain E1 which was isolated from Piper sarmentosum (Kadok) showed the highest specific activity against 1-chloro-2, 4-dinitrobenzene substrates (5.78 × 10-06 μmol/min/mg). Based on the carbon utilization of E1 assessed using Biolog system, the strain was identified as Comamonas testosterone E1. Glutathione S-transferase purification using GST trap yielded two distinct subunits with molecular weights of 23 and 24 kDa as visualized on 1D SDS-polyacrylamide gel electrophoresis. The purified GST showed reactivity towards 1-chloro-2, 4-dinitrobenzene, 1, 2-dichloro-4-nitrobenzene and ethacrynic acid with specific activity of 0.264 ± 0.038 nmol/min/mg and 0.056 ± 0.002 nmol/min/mg and 10.500 ± 3.130 nmol/min/mg, respectively. However, no activity was detected against p-Nitrobenzyl chloride, Sulfobromophthalein, trans-4-phenyl-3-butene-2-one, hexa-2, 4- dienal, trans-hepta-2, 4-dienal and trans-oct-2-enal in the study. Penerbit Universiti Kebangsaan Malaysia 2016-07 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/9979/1/07%20Khanom%20Simarani.pdf Khanom Simarani, and Wan Haizatul Akmal Che Yusoff, and Zazali Alias, (2016) Purification of glutathione Transferases (GSTs) from identified Rhizospheric bacteria. Sains Malaysiana, 45 (7). pp. 1057-1062. ISSN 0126-6039 http://www.ukm.my/jsm/english_journals/vol45num7_2016/contentsVol45num7_2016.html
repository_type	Digital Repository
institution_category	Local University
institution	Universiti Kebangasaan Malaysia
building	UKM Institutional Repository
collection	Online Access
language	English
description	The glutathione S-Transferase (GST) enzyme plays an important role in cellular detoxification. This multifunctional enzyme is involved in Phase II detoxification pathways that protect cellular macromolecules from being attacked by harmful compound. The study is an attempt to isolate glutathione transferase-expressing bacteria from the rhizospheric soil of selected herbal plants. Screening showed nine positive isolates out of twelve bacterial samples from a large microbial population in our soil collection. Crude extract from strain E1 which was isolated from Piper sarmentosum (Kadok) showed the highest specific activity against 1-chloro-2, 4-dinitrobenzene substrates (5.78 × 10-06 μmol/min/mg). Based on the carbon utilization of E1 assessed using Biolog system, the strain was identified as Comamonas testosterone E1. Glutathione S-transferase purification using GST trap yielded two distinct subunits with molecular weights of 23 and 24 kDa as visualized on 1D SDS-polyacrylamide gel electrophoresis. The purified GST showed reactivity towards 1-chloro-2, 4-dinitrobenzene, 1, 2-dichloro-4-nitrobenzene and ethacrynic acid with specific activity of 0.264 ± 0.038 nmol/min/mg and 0.056 ± 0.002 nmol/min/mg and 10.500 ± 3.130 nmol/min/mg, respectively. However, no activity was detected against p-Nitrobenzyl chloride, Sulfobromophthalein, trans-4-phenyl-3-butene-2-one, hexa-2, 4- dienal, trans-hepta-2, 4-dienal and trans-oct-2-enal in the study.
format	Article
author	Khanom Simarani, Wan Haizatul Akmal Che Yusoff, Zazali Alias,
spellingShingle	Khanom Simarani, Wan Haizatul Akmal Che Yusoff, Zazali Alias, Purification of glutathione Transferases (GSTs) from identified Rhizospheric bacteria
author_facet	Khanom Simarani, Wan Haizatul Akmal Che Yusoff, Zazali Alias,
author_sort	Khanom Simarani,
title	Purification of glutathione Transferases (GSTs) from identified Rhizospheric bacteria
title_short	Purification of glutathione Transferases (GSTs) from identified Rhizospheric bacteria
title_full	Purification of glutathione Transferases (GSTs) from identified Rhizospheric bacteria
title_fullStr	Purification of glutathione Transferases (GSTs) from identified Rhizospheric bacteria
title_full_unstemmed	Purification of glutathione Transferases (GSTs) from identified Rhizospheric bacteria
title_sort	purification of glutathione transferases (gsts) from identified rhizospheric bacteria
publisher	Penerbit Universiti Kebangsaan Malaysia
publishDate	2016
url	http://journalarticle.ukm.my/9979/ http://journalarticle.ukm.my/9979/ http://journalarticle.ukm.my/9979/1/07%20Khanom%20Simarani.pdf
first_indexed	2023-09-18T19:56:16Z
last_indexed	2023-09-18T19:56:16Z
_version_	1777406550353117184

Purification of glutathione Transferases (GSTs) from identified Rhizospheric bacteria

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