6th International Young Scientist Congress (IYSC-2020) will be Postponed to 8th and 9th May 2021 Due to COVID-19. 10th International Science Congress (ISC-2020).  International E-publication: Publish Projects, Dissertation, Theses, Books, Souvenir, Conference Proceeding with ISBN.  International E-Bulletin: Information/News regarding: Academics and Research

Production and Optimization of L-Glutaminase (EC. by Streptomyces griseus using Wheat bran under Statistical Designs

Author Affiliations

  • 1Bioprocess Laboratory, Department of Chemical Engineering, Annamalai University, Annamalai nagar, Tamil Nadu- 608 002, INDIA
  • 2Department of Chemical Engineering, Annamalai University, Annamalai nagar, Tamil Nadu- 608 002, INDIA

Res. J. Recent Sci., Volume 3, Issue (ISC-2013), Pages 310-318, (2014)


L-Glutaminase majorly produced by micro organism including bacteria, yeast and fungi. L-Glutaminase mainly catalyzes the hydrolysis of -amido bond of L-Glutamine. In this report, optimization of the culture medium for L-Glutaminase production using Streptomyces griseus was carried out. The optimization of L-Glutaminase production using Wheat bran as substrate was performed with statistical methodology based on experimental designs. The screening of ten nutrients for their influence with Wheat bran on L-Glutaminase production is achieved using Plackett-Burman design. The basal medium contained Peptone 30 g/L, Ferrous sulphate 0.7 g/L, KH2PO4 0.7 g/L, NaCl 40 g/L was selected based on their higher influence on L-Glutaminase production. After medium components optimization, the temperature, pH, time, composition of the wheat bran, and inoculum size was optimized using response surface methodology (RSM). The predicted optimum levels are as follows: temperature 30.12o0, pH 8.36, time 117.11 h, wheat bran 33.60 g/L and inoculum size 0.90 %. This medium components and parameters were projected theoretically to produce an L-Glutaminase activity of 1959.99 IU/ml. The used methodology was validated using this optimized media components and parameters; the L-Glutaminase activity 1943.5 IU/ml was obtained.


  1. Brosnan J.T., Ewart H.S. and Squires S.A., Hormonal control of hepatic glutaminase, Adv Enzyme Regul, 35, 131–146 (1995)
  2. Carter P. and Welbourne T.G., Glutamate transport regulation of renal glutaminase flux in vivo, J Physiol, 273, 521–527(1997)
  3. Padma I and Singhal R.S., Production of glutaminase (E.C. from Zygosaccharomycesrouxii: statistical optimization using response surface methodology, Bio resource Technology, 99, 4300–4307 (2007)
  4. Riberg B., Torgner I.A. and Kvamme E., The orientation of phosphate activated glutaminase in the inner mitochondrial membrane of synaptic and non-synaptic rat brain mitochondria, NeurochemInt, 27, 367–376 (1995)
  5. Zhao J., Lopez A.L., Erichsen D., Herek S., Cotter R.L., Curthoys N.P. and Zheng J., Mitochondrial glutaminase enhances extracellular glutamate production in HIV-1-infected macrophages: Linkage to HIV-1 associated dementia, J Neurochem, 88, 169–180 (2004)
  6. Roberts J., MacAllister T.W., Sethuraman N. and Freeman A.G., Genetically engineered glutaminase and its use in antiviral and anticancer therapy, US Patent, 6312939, (2001)
  7. Schmid F.A. and Roberts J., Antineoplastic and toxic effects of Acinetobacter and Pseudomonas glutaminase-asparaginases, Cancer Chemother Rep, 58, 829–840 (1974)
  8. Mulchandani A. and Bassi A.S., Determination of glutamine and glutamic acid in mammalian cell cultures using tetrathiafulvalene modified enzyme electrodes, Biosensor Bioelectron, 11, 271–280 (1996)
  9. Villarta R.L, Palleschi G., Suleiman A. and Guilbault G.G. Determination of glutamine in serum using an amperometric enzyme electrode, Electroanalysis, 4, 27–31 (1992)
  10. Sabu A., Keerthi T.R., Kumar S.R. and Chandrasekaran M., L-Glutaminase production by marine Beauveria sp. under solid state fermentation, Process Biochem, 35, 705–710 (2000b)
  11. Chou C.C. and Hwan C.H., Effect of ethanol on the hydrolysis of protein and lipid during the ageing of a Chinese fermented soya bean curd-sufu, J Sci Food Agric, 66, 393–398 (1994)
  12. Nakadai T. and Nasuno S., Use of glutaminase for soy sauce made by Koji or a preparation of proteases from Aspergillusoryzae, J Ferment Bioeng, 67, 158–162 (1989)
  13. Sabu A., Chandrasekaran M. and Pandey A., Biopotential of microbial glutaminases, Chem. Today, 18, 21–25 (2000)
  14. Tachiki T., Yamada T., Mizuno K., Ueda M., Shiode J. and Fukami H., -Glutamyl transfer reactions by glutaminase from Pseudomonas nitroreducens IFO 12694 and their application for the syntheses of theanine and –glutamylmethylamide, BiosciBiotechnol Biochem, 62, 1279–1283 (1998)
  15. Nagendra Prabhu G. and Chandrasekaran M., Impact of process parameters on L-glutaminase production by marine Vibrio costicolain solid state fermentation using polystyrene as an inert support, Process Biochemistry, 32, 285–289 (1997)
  16. Prakasham R.S., Rao Ch.S., Rao R.S., Lakshmi G.S. and Sarma P.N. L-asparaginase production by isolated Staphylococcus sp. – 6A: design of experiment considering interaction effect for process parameter optimization, J ApplMicrobiol, 102, 1382–1391, (2007a)
  17. Rathi P., Saxena R. and Gupta R., A novel alkaline lipase from Burkholderiacepacia for detergent formulation, Proc. Biochem, 37, 187–192 (2001)
  18. Park Y., Kang S., Lee J., Hong I. and Kim W., Xylanase production in solid state fermentation by Aspergillusniger mutant using statistical experimental designs, Appl. Microbiol. Biotechnol, 58, 761–766 (2002)
  19. Suresh Kumar S., Muthuvelayudham R. and Viruthagiri T., Statistical Optimization based Production of L-Glutaminase (EC.
  20. by Serratia marcescens under submerged Fermentation, Research Journal of Chemical Science, 3(6), 43-53 (2013)
  21. Cavalitto S.F. and Mignone C.F., Application of factorial and Doehlert designs for optimization of protopectinase production by a Geotrichumklebahnii strain, Proc. Biochem,42, 175–179(2007)
  22. Imada A, Igarasi S, Nakahama K, Isono M. Asparaginase and Glutaminase activities of microorganisms, J Gen Microbiol,76,85–99 (1973)