메뉴 건너뛰기




Volumn 46, Issue 6, 2011, Pages 1342-1349

Induction of NAD+ dependent alcohol dehydrogenases with activity towards long chain aliphatic alcohols in mesophilic, thermophilic and extreme thermophilic microorganisms

Author keywords

Alcohol dehydrogenase; Behenic acid; Lignoceric acid; Long chain fatty acids; Polycosanols; Thermus; Thermus thermophilus

Indexed keywords

ALCOHOL DEHYDROGENASE; BEHENIC ACID; LIGNOCERIC ACID; LONG CHAIN FATTY ACID; POLYCOSANOLS; THERMUS; THERMUS THERMOPHILUS;

EID: 79955611111     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2011.03.002     Document Type: Article
Times cited : (10)

References (24)
  • 1
    • 79955627181 scopus 로고    scopus 로고
    • Composiciones y métodos para el tratamiento de enfermedades gastrointestinales
    • Mexican Patent 06001477 A
    • Clymer J. Composiciones y métodos para el tratamiento de enfermedades gastrointestinales. Mexican Patent 06001477 A; 2006.
    • (2006)
    • Clymer, J.1
  • 2
    • 79955610507 scopus 로고    scopus 로고
    • High drug loaded injectable microparticle compositions and methods of treating opioid drug dependence
    • US Patent 7,041,320 B1
    • Nuwayser E. High drug loaded injectable microparticle compositions and methods of treating opioid drug dependence. US Patent 7,041,320 B1; 2006.
    • (2006)
    • Nuwayser, E.1
  • 3
    • 79955601116 scopus 로고    scopus 로고
    • Humectant and cosmetics and external preparations containing the same
    • European Patent 1,417,955
    • Fujino J, Yokohama-shi K. Humectant and cosmetics and external preparations containing the same. European Patent 1,417,955; 2004.
    • (2004)
    • Fujino, J.1    Yokohama-shi, K.2
  • 4
    • 79955626325 scopus 로고    scopus 로고
    • Cosmetic and dermatological preparations in the form of o/ω-emulsions containing sterols and/or C12-C40 fatty acids
    • US Patent 0037036 A1
    • Nielsen J, Raschke T, Riedel H. Cosmetic and dermatological preparations in the form of o/ω-emulsions containing sterols and/or C12-C40 fatty acids. US Patent 0037036 A1; 2005.
    • (2005)
    • Nielsen, J.1    Raschke, T.2    Riedel, H.3
  • 5
    • 79955583203 scopus 로고    scopus 로고
    • Fuel additives and compositions
    • US Patent 0254127 A1
    • Breakspear A, Caprotti R, Fava C. Fuel additives and compositions. US Patent 0254127 A1; 2006.
    • (2006)
    • Breakspear, A.1    Caprotti, R.2    Fava, C.3
  • 7
    • 79955591240 scopus 로고    scopus 로고
    • online accessed 30.07.08
    • Lee J. http://www.hbci.com/~wenonah/new/pnutskin.htm; 2008 [online accessed 30.07.08].
    • (2008)
    • Lee, J.1
  • 8
    • 0035240998 scopus 로고    scopus 로고
    • Oxidation of long chain primary alcohols to acids over the quaternaryammoniumperoxotungstophosphate catalyst system
    • Bi Y, Zhou M, Hu H, Wei C, Li W, Zhen K. Oxidation of long chain primary alcohols to acids over the quaternaryammoniumperoxotungstophosphate catalyst system. React Kinet Catal Lett 2001;72:73-82.
    • (2001) React Kinet Catal Lett , vol.72 , pp. 73-82
    • Bi, Y.1    Zhou, M.2    Hu, H.3    Wei, C.4    Li, W.5    Zhen, K.6
  • 9
    • 77953419718 scopus 로고    scopus 로고
    • The use of an ionic liquid catalyst for the oxidation of hydrophobic high molecular weight alcohols
    • Guajardo N, Santana J, Carlesi C. The use of an ionic liquid catalyst for the oxidation of hydrophobic high molecular weight alcohols. Inform Tecnol 2010;21:57-65.
    • (2010) Inform Tecnol , vol.21 , pp. 57-65
    • Guajardo, N.1    Santana, J.2    Carlesi, C.3
  • 10
    • 0025064579 scopus 로고
    • Long-chain alcohol dehydrogenase of Candida yeast
    • Ueda M, Tanaka A. Long-Chain alcohol dehydrogenase of Candida Yeast. Methods Enzymol 1990;188:171-5. (Pubitemid 20384896)
    • (1990) Methods in Enzymology , vol.188 , pp. 171-175
    • Ueda, M.1    Tanaka, A.2
  • 11
    • 58149305792 scopus 로고    scopus 로고
    • Effect of chain length on the activity of free and immobilized alcohol dehydrogenase towards aliphatic alcohols
    • Cea G, Wilson L, Bolivar JM, Markovits A, Illanes A. Effect of chain length on the activity of free and immobilized alcohol dehydrogenase towards aliphatic alcohols. Enzyme Microb Technol 2009;44:135-8.
    • (2009) Enzyme Microb Technol , vol.44 , pp. 135-138
    • Cea, G.1    Wilson, L.2    Bolivar, J.M.3    Markovits, A.4    Illanes, A.5
  • 12
    • 0142136150 scopus 로고    scopus 로고
    • Identification and Characterization of the CYP52 Family of Candida tropicalis ATCC 20336, Important for the Conversion of Fatty Acids and Alkanes to ω,β-Dicarboxylic Acids
    • DOI 10.1128/AEM.69.10.5983-5991.2003
    • Craft D, Madduri K, Eshoo M, Wilson R. Identification and characterization of the CYP52 family of Candida tropicalis ATCC 20336, important for the conversion of fatty acids and alkanes to ω,β-dicarboxylic acids. Appl Environ Microbiol 2003;69:5983-91. (Pubitemid 37280321)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.10 , pp. 5983-5991
    • Craft, D.L.1    Madduri, K.M.2    Eshoo, M.3    Wilson, C.R.4
  • 13
    • 0034759239 scopus 로고    scopus 로고
    • Microbial conversion of n-alkanes into glycolipid biosurfactants, mannosylerythritol lipids, by Pseudozyma (Candida antarctica)
    • DOI 10.1023/A:1012464717259
    • Kitamoto D, Ikegami T, Suzuki G, Takeyama Y, Idemoto Y, Koura N, Yanagishita H. Microbial conversion of n-alkanes into glycolipid biosurfactants, mannosylerythritol lipids, by Pseudozyma (Candida antarctica). Biotechnol Lett 2001;23:1709-14. (Pubitemid 33019901)
    • (2001) Biotechnology Letters , vol.23 , Issue.20 , pp. 1709-1714
    • Kitamoto, D.1    Ikegami, T.2    Suzuki, G.T.3    Sasaki, A.4    Takeyama, Y.-I.5    Idemoto, Y.6    Koura, N.7    Yanagishita, H.8
  • 14
    • 33846621913 scopus 로고    scopus 로고
    • Alkane hydroxylases involved in microbial alkane degradation
    • DOI 10.1007/s00253-006-0748-0
    • VanBeilen J, Funhoff E. Alkane hydroxylases involved in microbial alkane degradation. Appl Microbiol Biotechnol 2007;74:13-21. (Pubitemid 46183463)
    • (2007) Applied Microbiology and Biotechnology , vol.74 , Issue.1 , pp. 13-21
    • Van Beilen, J.B.1    Funhoff, E.G.2
  • 15
    • 35048822557 scopus 로고    scopus 로고
    • The alcohol dehydrogenase gene adhA in Corynebacterium glutamicum is subject to carbon catabolite repression
    • DOI 10.1128/JB.00791-07
    • Arndt A, Eikmanns B. The alcohol dehydrogenase gene adhA in Corynebacterium glutamicum is subject to carbon catabolite repression. J Bacteriol 2007;189:7408-16. (Pubitemid 47557357)
    • (2007) Journal of Bacteriology , vol.189 , Issue.20 , pp. 7408-7416
    • Arndt, A.1    Eikmanns, B.J.2
  • 16
    • 34648830898 scopus 로고    scopus 로고
    • Transcriptionally regulated adhA gene encodes alcohol dehydrogenase required for ethanol and n-propanol utilization in Corynebacterium glutamicum R
    • DOI 10.1007/s00253-007-1094-6
    • Kotrbova-Kozak A, Kotrba P, Inui M, Sajdok J, Yukawa H. Transcriptionally regulated adhA gene encodes alcohol dehydrogenase required for ethanol and n-propanol utilization in Corynebacterium glutamicum R. Appl Microbiol Biotechnol 2007;76:1347-56. (Pubitemid 47459769)
    • (2007) Applied Microbiology and Biotechnology , vol.76 , Issue.6 , pp. 1347-1356
    • Kotrbova-Kozak, A.1    Kotrba, P.2    Inui, M.3    Sajdok, J.4    Yukawa, H.5
  • 17
    • 18244426599 scopus 로고    scopus 로고
    • Degradation of tetrahydrofurfuryl alcohol by Ralstonia eutropha is initiated by an inducible pyrroloquinoline quinone-dependent alcohol dehydrogenase
    • Zarnt G, Schräder T, Andreesen J. Degradation of tetrahydrofurfuryl alcohol by Ralstonia eutropha is initiated by an inducible pyrroloquinoline quinine-dependent alcohol dehydrogenase. Appl Environ Microbiol 1997: 4891-8. (Pubitemid 27524228)
    • (1997) Applied and Environmental Microbiology , vol.63 , Issue.12 , pp. 4891-4898
    • Zarnt, G.1    Schrader, T.2    Andreesen, J.R.3
  • 18
    • 1842451878 scopus 로고    scopus 로고
    • Properties of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix K1
    • DOI 10.1263/jbb.97.202
    • Hirakawa H, Kamiya N, Kawarabayashi Y, Nagamune T. Properties of an alcohol dehydrogenase from the hyperthermophilic Archaeon Aeropyrum pernix K1. J Biosci Bioeng 2004;97:202-6. (Pubitemid 38457117)
    • (2004) Journal of Bioscience and Bioengineering , vol.97 , Issue.3 , pp. 202-206
    • Hirakawa, H.1    Kamiya, N.2    Kawarabayashi, Y.3    Nagamune, T.4
  • 19
    • 0344153755 scopus 로고    scopus 로고
    • Alcohol dehydrogenases from thermophilic and hyperthermophilic arquea and bacteria
    • Radianingtyas H, Wright P. Alcohol dehydrogenases from thermophilic and hyperthermophilic arquea and bacteria.FEMSMicrobiol Rev 2003;27:593-616.
    • (2003) FEMSMicrobiol Rev , vol.27 , pp. 593-616
    • Radianingtyas, H.1    Wright, P.2
  • 20
    • 33745711929 scopus 로고    scopus 로고
    • Influence of temperature on the production of an archaeal thermoactive alcohol dehydrogenase from Pyrococcus furiosus with recombinant Escherichia coli
    • DOI 10.1007/s00792-005-0490-z
    • Kube J, Brokamp C, Machielsen R, Van der Oost J, Märkl H. Influence of temperature on the production of an archaeal thermoactive alcohol dehydrogenase from Pyrococcus furiosus with recombinant Escherichia coli. Extremophiles 2006;10:221-7. (Pubitemid 44000101)
    • (2006) Extremophiles , vol.10 , Issue.3 , pp. 221-227
    • Kube, J.1    Brokamp, C.2    Machielsen, R.3    Van Der, O.J.4    Markl, H.5
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 22
    • 65549122434 scopus 로고    scopus 로고
    • Alkane inducible proteins in Geobacillus thermoleovorans B23
    • Kato T, Miyanaga A, Kanaya S. Morikawa. Alkane inducible proteins in Geobacillus thermoleovorans B23. BMC Microbiol 2009;9:60.
    • (2009) BMC Microbiol , vol.9 , pp. 60
    • Kato, T.1    Miyanaga, A.2    Kanaya, S.3    Morikawa4
  • 23
    • 0000084946 scopus 로고
    • Purification and properties of primary and secondary alcohol dehydrogenases from Thermoanaerobacter ethanolicus
    • Bryant F, Wiegel J, Ljungdahl L. Purification and properties of primary and secondary alcohol dehydrogenases from Thermoanaerobacter ethanolicus. Appl Environ Microbiol 1988;54:460-5.
    • (1988) Appl Environ Microbiol , vol.54 , pp. 460-465
    • Bryant, F.1    Wiegel, J.2    Ljungdahl, L.3
  • 24
    • 0026658917 scopus 로고
    • Comparison of alcohol dehydrogenases from wild-type and mutant strain JW200 Fe 4, of Thermoanaerobacter ethanolicus
    • Bryant F, Wiegel J, Ljungdahl L. Comparison of alcohol dehydrogenases from wild-type and mutant strain JW200 Fe 4, of Thermoanaerobacter ethanolicus. Appl Microbiol Biotechnol 1992;37:490-5.
    • (1992) Appl Microbiol Biotechnol , vol.37 , pp. 490-495
    • Bryant, F.1    Wiegel, J.2    Ljungdahl, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.