Recombinant Bacteria for Alkane Degradation

Due to multi-component nature, recombinant production of CYP450 is difficult, but CYP BM-3 is readily expressed in E. coli (Peter et al. 2003).

Rothen et al. (1998) constructed a plasmid with gene coding for the three enzymes; alkane hydroxylase, alcohol dehydrogenase and aldehyde dehydrogenase simultaneously. The plasmid was inserted into an E. coli strain unable to

Table 17.1 Different enzymes involved in alkane degradation (van Beilen et al. 2003)




Reference sMMO


Propane monooxygenase

Butane monooxygenase AlkB

Cytochrome P450 (CYP153) monooxygenase

Cytochrome P450 (CYP52) monooxygenase

Methylococcus capsulatus

Methylisinus trichosporum


All methanotrophs

Pseudomonas butanovora (ATCC 43655) Gordonia sp. TYP Acinetobacter, Alcanivorax, Burkholderia, Mycobacterium, Pseudomonas, Rhodococcus etc. Sphingomonas sp. HXN-200, Mycobacterium sp. HXN1500 Acinetobacter sp. EB104

Candida maltosa, Candida tropicalls, Yarrowia lipolytica




C3 and C13-C5-C16

Leieberman and Rosenzweig (2004) Kotani et al. (2003)



metabolize fatty acids. The recombinant bacteria were able to oxidize octane to its corresponding carboxylic acid.

Glieder et al. (2002) produced a mutant 139-3 that was capable to catalyze the oxidation of medium chain alkanes. This mutant has the fastest known enzyme for alkane hydroxylation (more than 17 times faster than the MMO or Alk enzymatic systems).

A plasmid having three components of Alk system was introduced to a Pseudomonas lacking the alcohol dehydrogenase. Now the recombinant bacteria were able to transform C7-C11 alkanes to their corresponding alcohols (Bosetti et al. 1992).

Throne-Holst et al. (2007) constructed alkMa, alkMb and alkMa/alkMb dist-ruption mutants of Acinetobacter venetianus 642. Single and double mutants were able to grow on n-alkanes (>C20).

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