Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 66, 2002 - Issue 4
Journal homepage
110
Views
9
CrossRef citations to date
0
Altmetric
Original Articles

Heterogeneity of Dehydrogenases of Stenotrophomonas maltophilia Showing Dye-linked Activity with Polypropylene Glycols

Shinjiro TACHIBANADepartment of Bioscience and Biotechnology, Faculty of Agriculture, University of the Ryukyus1 Senbaru, Nishihara-cho, Okinawa 903-0213, Japan
,
Fusako KAWAIResearch Institute for Bioresources, Okayama University2-20-1 Chuo, Kurashiki, Okayama 710-0046, Japan
&
Masaaki YASUDADepartment of Bioscience and Biotechnology, Faculty of Agriculture, University of the Ryukyus1 Senbaru, Nishihara-cho, Okinawa 903-0213, Japan
Pages 737-742 | Received 31 Aug 2001, Accepted 17 Dec 2001, Published online: 22 May 2014

  • 1) Kawai, F., Kimura, T., Tani, Y., Yamada, H., and Kurachi, M., Purification and characterization of polyethylene glycol dehydrogenase involved in the bacterial metabolism of polyethylene glycol. Appl. Environ. Microbiol., 40, 701-705 (1980).
  • 2) Kawai, F. and Enokibara, S., Role of novel dye-linked dehydrogenases in the metabolism of polyethylene glycol by pure cultures of Sphingomonas sp. N6. FEMS Microbiol. Lett., 141, 45-50 (1996).
  • 3) Yasuda, M., Cherepanov, A., and Duine, J. A., Polyethylene glycol dehydrogenase activity of Rhodopseudomonas acidophila derives from a type I quinohaemoprotein alcohol dehydrogenase. FEMS Microbiol. Lett., 138, 23-28 (1996).
  • 4) Shimao, M., Ninomiya, K., Kuno, O., Kato, N., and Sakazawa, C., Existence of a novel enzyme, pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase, in a bacterial symbiont, Pseudomonas sp. strain VM15C. Appl. Environ. Microbiol., 51, 268-275 (1986).
  • 5) Hatanaka, T., Asahi, N., and Tsuji, M., Purification and characterization of poly(vinyl alcohol) dehydrogenase from Pseudomonas sp.113P3. Biosci. Biotechnol. Biochem., 59, 1813-1816 (1995).
  • 6) Matsumura, S., Tomizawa, N., Toki, A., Nishikawa, K., and Toshima, K., Novel poly(vinyl alcohol)- degrading enzyme and the degradation mechanism. Macromolecules., 32, 7753-7761 (1999).
  • 7) Kawai, F., Hanada, K., Tani, Y., and Ogata, K., Bacterial degradation of water-insoluble polymer (polypropylene glycol). J. Ferment. Technol., 55, 89-96 (1977).
  • 8) Kawai, F., Okamoto, T., and Suzuki, T., Aerobic degradation of polypropylene glycol by Corynebacterium sp. J. Ferment. Technol., 63, 239-244 (1985).
  • 9) Gerhardt, P., Murray, R. G. E., Costilow, R. N., Nester, E. W., Wood, W. A., Krieg, N. R., and Phillips, G. B., Manual of methods for general bacteriology. American society for microbiology, Washington, DC., pp. 26-27 (1981).
  • 10) Groen, B. W., and Duine, J. A., Quinoprotein alcohol dehydrogenase from Pseudomonas aeruginosa and quinohemoprotein alcohol dehydrogenase from Pseudomonas testosteroni. Meth. Enzymol., 188, 33-39 (1990).
  • 11) Anraku, Y., and Heppel, L. A., On the nature of the changes induced in Escherichia coli by osmotic shock. J. Biol. Chem., 242, 2561-2569 (1967).
  • 12) Bergmeyer, H. U., Gowehn, K., and Grassl, M., Enzymes as biochemical reagents. Methods of enzymatic analysis, 2 nd. Ed. Academic Press, Inc., New York., pp. 425-522 (1974).
  • 13) Brown, E. G. and Hayes, T. J., The absorptiometric determination of polyethyleneglycol mono-oleate. Analyst, 80, 755-767 (1955).
  • 14) Davis, B. J., Disc electrophoresis. II. Method and application to human serum proteins. Ann. N.Y. Acad. Sci., 121, 404-427 (1964).
  • 15) Shimao, M., Nishimura, Y., Kato, N., and Sakazawa, C., Localization of polyvinyl alcohol oxidase produced by a bacterial symbiont, Pseudomonas sp. strain VM15C. Appl. Environ. Microbiol., 49, 8-10 (1985).
  • 16) Obradors, N. and Aguilar, J., Efficient biodegradation of high-molecular-weight polyethylene glycols by pure cultures of Pseudomonas stutzeri. Appl. Environ. Microbiol., 57, 2383-2388 (1991).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.