Production of Microbial-Transglutaminase [MTG] from Streptoverticillium mobaraense

  • Wang, Hong-Wei (Department of Bioscience and Biotechnology, College of Engineering, Silla University) ;
  • Kim, In-Hae (Department of Pharmaceutical Engineering, College of Medical Life Science, Silla University) ;
  • Park, Chang-Su (Department of Pharmaceutical Engineering, College of Medical Life Science, Silla University) ;
  • Lee, Jae-Hwa (Department of Bioscience and Biotechnology, College of Engineering, Silla University)
  • Published : 2007.10.30

Abstract

Mineral salts in medium usually profoundly influence microorganism growth and protein synthesis. In order to produce microbial transglutaminase (MTG) with a high yield from Streptoverticillium mobaraense, we screened the minerals $CaCl_2,\;CoCl_2,\;FeSO_4,\;ZnSO_4,\;MnSO_4\;and\;CuSO_4$ for MTG fermentation. The results indicated that appropriate $FeSO_4$ concentrations could significantly promote cell growth and stimulate the production of MTG. With 15 mg/L of $FeSO_4$ added to medium, 58% improvements were noted in MTG productivity (2.24 U/mL). NaCl, $CaCl_2,\;and\;CoCl_2$ enhanced MTG productivity by less than 15%, and the optimal concentrations were determined as 1 g/L, 2 g/L, and 30 mg/L respectively. Furthermore, it was determined that 7.5 mg/L of $ZnSO_4$ in medium could augment MTG productivity by 20% and induce the stationary phase for MTG production to a period 24 hr earlier. This basic and novel discovery should result in the development of a good complement to the previously defined culture media for MTG fermentation.

Keywords

References

  1. Nonaka, M., H. Tanaka, A. Okiyama, M. Motoki, H. Ando, K. Umeda, and A. Matsumura (1989), Polymerization of several proteins by $Ca^{2+}$-independent derived transglutaminase from microorganism, Agric. Biol. Chem. 53, 2619-2623 https://doi.org/10.1271/bbb1961.53.2619
  2. Zhu, Y., A. Rinzema, J. Tramper, and J. Bol (1995), Microbial transglutaminasea review on its production and application in food processing, Appl. Microbiol. Biotechnol. 44, 277-282 https://doi.org/10.1007/BF00169916
  3. Motoki, M. and K. Seguro (1994), Trends in Japanese soy protein research, Inform 5, 308-313
  4. Steinknaus, K. H (1994), Nutritional significance of fermented foods, Food Res. Int. 27, 259-267 https://doi.org/10.1016/0963-9969(94)90094-9
  5. Ando, H., M. Adachi, K. Umeda, A. Matsuura, M. Nonaka, and R. Uchio (1989), Purification and characterization of a novel transglutminase derived from microorganism, Agric. Biol. Chem. 53, 2613-2617 https://doi.org/10.1271/bbb1961.53.2613
  6. Zhu, Y., A. Rinzema, and J. Tramper (1996), Medium design based on stoichiometric analysis of microbial transglutaminase production by Streptoverticillium mobaraense, Biotechnol. Bioeng. 50, 291-298
  7. Junqua, M., R. Duran, C. Gancet, and R. Goulas (1997), Optimization of microbial transglutaminase production using experimental designs, Appl. Microbiol. Biotechno. 6, 730-734
  8. Zhu, Y., A. Rinzema, and J. Tramper (1998), Fed-batch fermentation dealing with nitrogenlimitation in microbial transglutaminase production by Streptoverticillium mobaraense, Bitechnol. Bioeng. 3, 251-257
  9. Zhu, Y., A. Rinzema, and J. Tramper (1998), Microbial transglutaminase production by: Streptoverticillium mobaraense analysis of amino acid metabolism using mass balances, Enzym. Microb. Technol. 3, 216-226
  10. Zheng, M. Y., G. C. Du, F. Wang, and J. Chen (2000), A temperature-shift strategy in batch microbial transglutaminase fermentation, Pro. Biochem. 36, 525-530
  11. Guo, L. Y., G. C. Du, Y. Li, J. Chen, and J. J. Zhong (2005), Enhancement of microbial transglutaminase production by Streptoverticillium mobaracnsc: application of a two stage agitation speed control strategy, Pro. Biochem. 40, 963-968 https://doi.org/10.1016/j.procbio.2004.04.002
  12. Zheng, M. Y., G. C. Du, and J. Chen (2002), pH control strategy of batch microbial transglutaminase production with Streptoverticillium mobaraense, Enzyme Microb. Technol. 31, 477-481 https://doi.org/10.1016/S0141-0229(02)00127-8
  13. Gerber, U, U. J. Nischke, S. Putzien, and H. L. Puchsbauer (1994), A rapid and simple method for the purification of transglutaminase from Streptoverticillium mobaraence, Biochem. J. 299, 825-829 https://doi.org/10.1042/bj2990825
  14. Grossowicz, N., E. Wainfan, E. Borek, and H. Waelsch (1950), The enzymatic of formation hydroxamic acids from glutamine, J. Bioi. Chem. 187, 111-125
  15. Miller, G. L. and C. Cased (1959), Use of dinitrosalicylic acid reagent for determination of reducing sugar, Anal. Chem. 31, 426-428 https://doi.org/10.1021/ac60147a030
  16. Eckhard, K. and H. G. Loffler (1981), Studies on the $Zn^{2+}/Co^{2+} $exchange with from pig aminoacylase kidney, Z. Natureforsch. 30, 951-955
  17. Hwang, D. Y. and I. B. Faramarz (2002), Glucose uptake and lactate production in cells exposed to $CoCl_2$ and in cell overpressing the Glut-l glucose transporter, Arch. Biochem. Biophy. 399, 206-211 https://doi.org/10.1006/abbi.2002.2758