Expression, purification and characterization of meta-cleavage enzyme CarBaBb froim Novosphiongobium sp. K

Zulkharnain, A.B and Maeda, R. and Omori, T. (2013) Expression, purification and characterization of meta-cleavage enzyme CarBaBb froim Novosphiongobium sp. K. Journal of biochemistry, microbiology and biotechnology, 1 (1). pp. 11-16. ISSN 2289-5779

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Abstract

The meta-cleavage enzyme carbabb of carbazole-degrader novosphiongobium sp. Ka1 werecloned, expressed and purified to homogeneity in escherichia coli strain. The enzyme was cloned with 6x histidine residues attached at the c-terminal of large subunit carbb for purification using affinity chromatography methodprior to gel filtration chromatography. The carbabb, a two-subunit meta-cleavage enzyme, approximately 30 kda for carbb dan 10 kda for carba, was found to be α2β2-heterotetrameric (mr 80,000), showed highest activity at ph 8.5 and temperature 30°c. Carbabb showed highest catalytic activity towards 2,3-dihydroxybiphenyl with kcat/km 4.1 m-1s-1, and overall higher catalytic activities towards biphenyl-type substrates in comparison to catechol-type substrates.Based on the similarities, this meta-cleavage enzyme fromnovosphiongobium sp. Ka1 would also be a good candidate for protein crystallization and structural studies apart from carbabb from strain p. Resinovorans strain ca10.

Item Type: Article
Additional Information: Universiti Malaysia Sarawak, UNIMAS
Uncontrolled Keywords: meta-cleavage enzyme, extradiol dioxygenase, carbazole degradation, CarBaBb, Novosphiongobium sp.K, FSTS, 2013, Universiti Malaysia Sarawak, UNIMAS, universiti, university, Borneo, Malaysia, Sarawak, Kuching, Samarahan, IPTA, education, research
Subjects: Q Science > Q Science (General)
Q Science > QR Microbiology
Divisions: Academic Faculties, Institutes and Centres > Faculty of Resource Science and Technology
Depositing User: Karen Kornalius
Date Deposited: 28 Mar 2014 08:01
Last Modified: 30 Apr 2021 05:03
URI: http://ir.unimas.my/id/eprint/1571

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