Cloning and expression of alkane hydroxylase-1 from Alcanivorax borkumensis in Escherichia coli.

Abstract:

:Enzymes with hydroxylating activity on alkanes have potential application as biotransformation catalysts in chemical and pharmaceutical industry. Genome of Alcanivorax borkumensis, a marine bacterium with hydrocarbon dissimilation activity, contains at least two P450 monooxygenases and two nonheme monooxygenases, AlkB1 and AlkB2, respectively. Presumably, all these enzymes possess alkane hydroxylating activity. Both AlkB1 and AlkB2 are membrane proteins. Two accessory proteins, rubredoxin and rubredoxin reductase, supply the reducing equivalent from nicotinamide adenine dinucleotide phosphate reduced (NADPH to hydroxylases. Rubredoxin reductase catalyses the reduction of rubredoxin by oxidation of NADPH, and rubredoxin transfers the electrons to the alkane hydroxylase to complete the hydroxylation reaction. Here, we sought to investigate the expression of alkB1 gene in Escherichia coli. Therefore, we amplified alkB1 gene from A. borkumensis genome by polymerase chain reaction and cloned it in the expression vector pET26 upstream of His-tag sequence. Predisposed BL21 (DE3) cells were transformed by the recombinant vector. At last, expression of recombinant enzyme was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting. Regarding the potential ability of this enzyme in hydroxylation of long-chained alkanes, the application of it would be studied in petroleum downstream industries.

journal_name

Toxicol Ind Health

authors

Eidani SZ,Shahraki MK,Gasemisakha F,Hahsemi M,Bambai B

doi

10.1177/0748233711416953

subject

Has Abstract

pub_date

2012-07-01 00:00:00

pages

560-5

issue

6

eissn

0748-2337

issn

1477-0393

pii

0748233711416953

journal_volume

28

pub_type

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