A Potential Use Of Dehalogenase D (Dehd) From Rhizobium Sp. For Industrial Process

The Rhizobium sp. DehL and DehD were produced by heterologous expression of the cloned gene in E.coli and both proteins purified using anion-exchange column chromatography. DehL and DehD were characterised by kinetic analysis to determine their Km, Kcat and the Specificity constant values. The kinet...

Full description

Bibliographic Details
Main Authors: Huyop, Fahrul Z., Ronald, A. Cooper
Format: Article
Language:English
Published: Penerbit UTM Press 2003
Subjects:
Online Access:http://eprints.utm.my/1467/
http://eprints.utm.my/1467/1/JT38C%5B7%5D.pdf
_version_ 1848890144681099264
author Huyop, Fahrul Z.
Ronald, A. Cooper
author_facet Huyop, Fahrul Z.
Ronald, A. Cooper
author_sort Huyop, Fahrul Z.
building UTeM Institutional Repository
collection Online Access
description The Rhizobium sp. DehL and DehD were produced by heterologous expression of the cloned gene in E.coli and both proteins purified using anion-exchange column chromatography. DehL and DehD were characterised by kinetic analysis to determine their Km, Kcat and the Specificity constant values. The kinetic analysis results showed that DehD from Rhizobium sp. has lower Km value (0.04 mM with D,L-2-CP) and higher Kcat (6.28 sec–1 for D,L-2-CP) and Specificity constants (1.46 × 105 M–1sec–1 for D,L-2-CP) compared to other D-specific dehalogenases from different organism suggesting DehD enzyme from Rhizobium sp. is better catalysts. D-2-haloacid dehalogenase is important for industrial biocatalysis compared to the L-2-haloacid and the kinetic data of DehD hold promise for further development to be used in an industrial process.
first_indexed 2025-11-15T20:37:24Z
format Article
id utm-1467
institution Universiti Teknologi Malaysia
institution_category Local University
language English
last_indexed 2025-11-15T20:37:24Z
publishDate 2003
publisher Penerbit UTM Press
recordtype eprints
repository_type Digital Repository
spelling utm-14672017-11-01T04:17:41Z http://eprints.utm.my/1467/ A Potential Use Of Dehalogenase D (Dehd) From Rhizobium Sp. For Industrial Process Huyop, Fahrul Z. Ronald, A. Cooper QH301 Biology The Rhizobium sp. DehL and DehD were produced by heterologous expression of the cloned gene in E.coli and both proteins purified using anion-exchange column chromatography. DehL and DehD were characterised by kinetic analysis to determine their Km, Kcat and the Specificity constant values. The kinetic analysis results showed that DehD from Rhizobium sp. has lower Km value (0.04 mM with D,L-2-CP) and higher Kcat (6.28 sec–1 for D,L-2-CP) and Specificity constants (1.46 × 105 M–1sec–1 for D,L-2-CP) compared to other D-specific dehalogenases from different organism suggesting DehD enzyme from Rhizobium sp. is better catalysts. D-2-haloacid dehalogenase is important for industrial biocatalysis compared to the L-2-haloacid and the kinetic data of DehD hold promise for further development to be used in an industrial process. Penerbit UTM Press 2003-06 Article PeerReviewed application/pdf en http://eprints.utm.my/1467/1/JT38C%5B7%5D.pdf Huyop, Fahrul Z. and Ronald, A. Cooper (2003) A Potential Use Of Dehalogenase D (Dehd) From Rhizobium Sp. For Industrial Process. Jurnal Teknologi C (38C). pp. 69-75. ISSN 0127-9696
spellingShingle QH301 Biology
Huyop, Fahrul Z.
Ronald, A. Cooper
A Potential Use Of Dehalogenase D (Dehd) From Rhizobium Sp. For Industrial Process
title A Potential Use Of Dehalogenase D (Dehd) From Rhizobium Sp. For Industrial Process
title_full A Potential Use Of Dehalogenase D (Dehd) From Rhizobium Sp. For Industrial Process
title_fullStr A Potential Use Of Dehalogenase D (Dehd) From Rhizobium Sp. For Industrial Process
title_full_unstemmed A Potential Use Of Dehalogenase D (Dehd) From Rhizobium Sp. For Industrial Process
title_short A Potential Use Of Dehalogenase D (Dehd) From Rhizobium Sp. For Industrial Process
title_sort potential use of dehalogenase d (dehd) from rhizobium sp. for industrial process
topic QH301 Biology
url http://eprints.utm.my/1467/
http://eprints.utm.my/1467/1/JT38C%5B7%5D.pdf