Advanced search×

Degradation of car engine base oil by Rhodococcus sp. NDKK48 and Gordonia sp. NDKY76A.

Daisuke D Koma, Yuichi Y Sakashita, Kenzo K Kubota, Yoshihide Y Fujii, Fumihiko F Hasumi, Seon-Yong SY Chung, and Motoki M Kubo

Biosci Biotechnol Biochem 67(7):1590-3 (2003) PMID 12913308

Two microorganisms (NDKK48 and NDKY76A) that degrade long-chain cyclic alkanes (c-alkanes) were isolated from soil samples. Strains NDKK48 and NDKY76A were identified as Rhodococcus sp. and Gordonia sp., respectively. Both strains used not only normal alkane (n-alkane) but also c-alkane as a sole carbon and energy source, and the strains degraded more than 27% of car engine base oil (1% addition).

Version: za2963e q8za5 q8zb2 q8zcc q8zdb q8ze7 q8zf1 q8zg4

Similar articles you may find interesting…

  1. Evidence that clustered phosphocholine head groups serve as sites for binding and assembly of an oligomeric protein pore.
    Angela A Valeva, Nadja N Hellmann, ... Sucharit S Bhakdi

    J Biol Chem 281(36):26014-21 (2006) PMID 16829693

    We propose that low affinity binding moieties can assume the role of high affinity binding sites due to their spatial arrangement in the membrane. Evidence is presented that phosphocholine head groups of sphingomyelin, clustered in sphingomyelin-cholesterol microdomains, serve this function for alph...
    PDF not found
  2. CT imaging with iopromide liposomes in a rabbit model.
    Werner Krause, Alexander Schönborn, and Karsten Rupp

    J Liposome Res 21(3):229-36 (2011) PMID 21039317

    The aim of this study was to evaluate the computed tomography (CT)-imaging potential of iopromide-carrying liposomes (SPC/CH/SPG, 6:3:1) of approximately 200 nm in diameter in healthy rabbits and in rabbits with implanted liver tumors in an intraindividual comparison with iopromide...
  3. Caveolin-1 binding motif of alpha-hemolysin: its role in stability and pore formation.
    Satyabrata S Pany, Ravi R Vijayvargia, and M V MV Krishnasastry

    Biochem Biophys Res Commun 322(1):29-36 (2004) PMID 15313169

    We have identified a nine amino sequence in alpha-hemolysin (alpha-HL) of Staphylococcus aureus, which binds Caveolin-1. Surface plasmon resonance studies clearly show a concentration dependent interaction of alpha-HL with the scaffolding domain of Caveolin-1. Mutants of alpha-HL, devoid of Caveolin...