PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2009 | 59 | 3 |
Tytuł artykułu

Glutamine amidohydrolase from Penicillinum politans NRC 510

Treść / Zawartość
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
Glutamine deamidating enzyme from Penicillium politans NRC510 catalyzed deamidation of glutamine to glutamic acid and ammonia. The enzyme was partially purified by a simple method of heating and Sephadex G-100 gel filtration. This procedure yields the partially purified enzyme with a 25% recovery of the activity in crude extracts. Specific activity of this partially purified enzyme is 133 U/mg. The partially purified enzyme hydrolyzes L-glutamine, D-glutamine L-asparagine and D-asparagine, while it cannot hydrolyze the other amide such as nicotinamide adenine dinucleotide, nicotinamide and acetamide under the same experimental conditions. The purified enzyme showed the maximal activity against L-glutamine at pH 7.5-8.5 and 60°C. The enzyme has a high salt tolerance, that shows high activity (75% of the original activity) in the presence of 15-30% NaCl. Exposure of the partially purified enzyme to 60°C for 30 min in the absence of the substrate, has no effect on its activity. While it was inhibited to a variable extent by addition of some substances such as HgCl2, NaF, CaCl2, BaCl2 and CuSO4 but was not affected by 2-merceptoethanol and iodoacetate. Product inhibition was recorded by addition of glutamic acid or NH3 to the reaction mixture. Glutamic acid inhibition was a competitive type and the km and the ki values were found to be 7.5 and 39.0 mol/L, respectively.
Słowa kluczowe
Wydawca
-
Rocznik
Tom
59
Numer
3
Opis fizyczny
p.211-217,fig.,ref.
Twórcy
autor
  • Microbial Chemistry Department, National Research Centre, El-Behoos Street, Dokki, Cairo, Egypt
autor
  • Microbial Chemistry Department, National Research Centre, El-Behoos Street, Dokki, Cairo, Egypt
  • Microbial Chemistry Department, National Research Centre, El-Behoos Street, Dokki, Cairo, Egypt
Bibliografia
  • 1. Ali T.H., Elsayed S.T., Optimization of cultural conditions for formation of L-asparagine deamidating enzyme by Penicillium politans NRC 510. New Egyp. J. Microbiol., 2006, 15, 62–74.
  • 2. Bhattacharya P,, Sett S,, Maity P., Effect of purified glutaminase from human ascites fluid on experimental tumor bearing mice. J. Exp. Clin. Cancer Res., 2001, 20, 599–607.
  • 3. Borek D., Michalska K., Brzezinski K., Kisiel A., Podkowinski J., Bonthron D.T., Krowarsch D., Otlewski J., Jaskolski M., Expression, purification and catalytic activity of Lupinus luteus asparagine β-amidohydrolase and its Escherichia coli homolog. Eur. J. Biochem., 2004, 271, 3215–3226.
  • 4. Calderon-Flores A., Pont G.D., Huerta-Saquero A., Merchant-Larios H., Servin-Gonzalez L., Duran S., The stringent response is required for amino acid and nitrate utilization, nod factor regulation, nodulation, and nitrogen fixation in Rhizobium etli. J Bacteriol., 2005, 187, 5075–5083.
  • 5. Dharmaraj K., Selvakumar D., Chandramohan D., Natarajan R., L-glutaminase in marine sediments. Indian J. Mar. Sci., 1977, 6, 168–1670.
  • 6. Duran S., Sanchez L.L., Huerta S.A., Pont G.D., Huerta Z.A., Calderon J., Du P.G., Identification of two glutaminases in Rhizobium etli. Biochem. Genetics, 1996, 34, 453–465.
  • 7. Elzainy T.A., Ali T.H., Detection of the antitumor glutaminase-asparaginase in the filamentous fungi. J. Appl. Sci., 2006, 6, 1389–1395.
  • 8. Huerta-Saquero A., Carderon J., Arreguin R., Calderon-Flores A., Duran S., Over expression and purification of Rhizobium etli glutaminase A by recombinant and conventional procedures. Protein Express. Purif., 2001, 21, 432.
  • 9. Huerta-Zepeda A., Ortuno L., Pont G., Duran S., Lloret A.M., Merchant-Larios H., Calderon J., Isolation and characterization of Rhizobium etli mutants altered in degradation of asparagine. J. Bacteriol., 1997, 179, 2068–2072.
  • 10. Ito K., Matsushita K., Koyama Y., Purification and characterization of a novel glutaminase of Aspergillus sojae (in Japanese). 2002, in: Proceedings of the Annual Meeting of the Society for Biotechnology, Japan. 2002, p. 135.
  • 11. Jackson C.M., Pautler E., Lavine K., Varian ‘Instruments at Work’, UV-1 4, 1981.
  • 12. Kennedy S.P., Wailap V.N.G., Salzberg S.L., Hood L., DasSarma S., Understanding the adaptation of Halobacterium species NRC-1 to its extreme environment through computational analysis of its genome sequence. Genome Res., 2001, 11, 1641–1650.
  • 13. Madern D., Ebel D., Zaccai D.G., Halophilic adaptation of enzymes. Extremophiles, 2000, 4, 91–98.
  • 14. Moriguchi M., Sakai K., Tateyama R., Furuta Y, Wakayama M., Isolation and characterization of salt-tolerant glutaminases from marine Micrococcus luteus K-3. J. Ferment. Bioeng., 1994, 77, 621–625.
  • 15. Nandakumar R., Yoshimune K., Wakayama M., Moriguchi M., Microbial glutaminase: biochemistry, molecular approaches and applications in the food industry. J. Molecular Catalysis B: Enzymatic, 2003, 23, 87–100.
  • 16. Ohnistti S.T., Barr J.K., A simplified method of quantitating protein. The Biuret and phenol reagents. Anal. Biochem., 1978, 86, 193–200.
  • 17. Ohshita K., Nakajima Y., Yamakoshi J., Kataoka S., Kikuchi M., Pariza M.W., Safety evaluation of yeast glutaminase. Food Chem. Toxicol., 2000, 38, 661–670.
  • 18. Prusiner S., Davis J. N., Stadtman E.P., Purification properties and cold lability. J. Biol.. Chem., 1976, 251, 3447–3456.
  • 19. Rath C.C., Subramanyam V.R., Thermotolerant enzyme activities of Bacillus species isolated from the hot springs of Orissa. Microbioscience, 1996, 86, 348, 157–161.
  • 20. Roberts J., Holcenberg J. S., Dolowy W.C., Antineoplastic activity of highly purified bacterial glutaminases. Letters to Nature, 1970, 1136–1137.
  • 21. Roberts J., Holcenberg J.S., Dolowy W.C., Isolation, crystallization and properties of Achromobacteraceae glutaminase–asparaginase with antitumor activity. J. Biol. Chem., 1972, 247, 84–90.
  • 22. Sabu A., Keerthi T.R.S., Rajeev Kumar S., Chandrasekaran M., Glutaminase production by marine Beauveria sp. under solid state fermentation. Process Biochem., 2000, 35, 705–710.
  • 23. Sato I., Kobayashi H., Hanya Y., Abe K., Murakami S., Scorzetti G., Fell J.W., Cryptococcus nodaensis sp nov, a yeast isolated from soil in Japan that produces a salt-tolerant and thermostable glutaminase. J. Indust. Microbiol. Biotechnol., 1999, 22, 127–132.
  • 24. Shimizu Y., Ueyama A., Goto K., Purification and characterization of glutaminase from Bacillus subtilis GT strain. J. Brew. Soc. Jpn., 1991, 66, 441–446.
  • 25. Soberon M., Gonzalez A., Physiological role of glutaminase activity in Saccharomyces cerevisiae. J. Gen. Microbiol., 1987, 133, 1–8.
  • 26. Sonawane A., Klo-ppner U., Derst C., Rohm K.H., Utilization of acidic amino acids and their amides by pseudomonads: role of periplasmic glutaminase-asparaginase. Arch. Microbiol., 2003, 179, 151–159.
  • 27. Steckel J., Roberts J., Philips F.S, Chou T.C., Kinetic properties and inhibition of Acinetobacter glutaminase – asparaginase. Biochem. Pharmacol., 1983, 32, 971–977.
  • 28. Thammarongtham C.T., Urner G., Moir A.J., Tanticharoen M., Cheevadhanarak S., A new class of glutaminase from Aspergillus oryzae. J. Mol. Microbiol. Biotechnol., 2001, 3, 611–617.
  • 29. Wakayama M., Yamagata T., Kamemura A., Bootim N., YanoS., Tachiki T., Yoshimune K., Moriguchi M., Characterization of salt-tolerant glutaminase from Stenotrophomonas maltophilia NYW-81 and its application in Japanese soy sauce fermentation. J. Ind. Microbiol. Biotechnol., 2005, 32, 383–390.
  • 30. Yano T., Ito M., Tomota K., Kumagai H., Tochikura T., Purification and properties of glutaminase from Aspergillus oryzae. J. Ferment. Technol., 1988, 66, 137–143.
  • 31. Yokotsuka T., Iwasa T., Fujii S., Species cryptococcus nodaensis, a process for producing salt-resistant thermostable glutaminase by use of the same, and a process for producing glutamic acid-rich protein hydrolysates. Nippon Shoyu Kenkyusho Zasshi., 1987, 13, 18–25.
Uwagi
rekord w opracowaniu
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.agro-02bf864a-7264-420f-bc07-5c75a94ac3bc
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.