406
Views
12
CrossRef citations to date
0
Altmetric
Articles

Optimization of culture conditions and bench-scale production of anticancer enzyme L-asparaginase by submerged fermentation from Aspergillus terreus CCT 7693

ORCID Icon, , , , &
Pages 95-104 | Received 05 Aug 2018, Accepted 14 Oct 2018, Published online: 29 Nov 2018

References

  • Costa-Silva, T.A.; Flores-Santos, J.C.; Freire, R.K.B.; Vitolo, M.; Pessoa, A. Jr, Microbial Cell Disruption Methods for Efficient Release of Enzyme L-Asparaginase. Prep. Biochem. Biotechnol. 2018, 6068, 1–11.
  • Avramis, V.I. Asparaginases: Biochemical Pharmacology and Modes of Drug Resistance. Anticancer Res. 2012, 32, 2423–2437.
  • Costa, I.M.; Schultz, L.; Araujo, B.P.B.; Leite, M.S.M.; Farsky, S.H.; Oliveira, M.; Pessoa-Jr, A.; Monteiro, G. Recombinant L-Asparaginase 1 from Saccharomyces cerevisiae: An Allosteric Enzyme with Antineoplastic Activity. Sci. Rep. 2016, 6, 36239.
  • Tareke, E.; Rydberg, P.; Karlsson, P.; Eriksson, S.; Törnqvist, M. Acrylamide: A Cooking Carcinogen? Chem. Res. Toxicol. 2000, 13, 517–522.
  • Clementi, A. La Desemidation Enzymatique de L-Asparagine Chez Les Differentes Especes Animales et la Signification Physiologique de as Presence Dans l Organisma. Arch. Int. Physiol. 1922, 19, 369–376.
  • Kidd, J. Regression of Transplanted Lymphomas Induced In Vivo by Means of Normal Guinea Pig Serum. I. Course of Transplanted Cancers of Various Kinds in Mice and Rats Given Guinea Pig Serum, Horse Serum, or Rabbit Serum. J. Exp. Med. 1953, 98, 565–582.
  • Broome, J.D. Evidence That the l-Asparaginase Activity in guinea Pig Serum is Responsible for its Antilymphoma Effects. Nature 1961, 191, 1114–1115.
  • Willis, R.C.; Woolfolk, R. Asparagine Utilization in Escherichia coli. J. Bacteriol. 1974, 118, 231–241.
  • Nagarethinam, S.; Nagappa, A.N.; Udupa, N.; Venkata, R.J.; Meenashi, B. Microbial L-Asparaginase and its Future Prospects. Asian J. Med. Res. 2012, 1, 159–168.
  • Sarquis, M.I.; Oliveira, E.M.; Santos, A.S.; Costa, G.L. Production of L-Asparaginase by Filamentous Fungi. Mem. Inst. Oswaldo Cruz 2004, 99, 489–492.
  • Loureiro, C.B.; Borges, K.S.; Andrade, A.F.; Tone, L.G.; Said, S. Biochemical Caracterization of Native and Pegylated Form of L-Asparaginase Produced by Aspergillus terreus: Evaluation in Vitro of Antineoplasic Activity. Aim 2012, 02, 138–145.
  • Cui, J.; Goh, K.K.T.; Archer, R.; Singh, H. Characterisation and Bioactivity of Protein-Bound Polysaccharides from Submerged-Culture Fermentation of Coriolus Versicolor Wr-74 ATCC-20545 Strains. J. Ind. Microbiol. Biotechnol. 2007, 34, 393–402.
  • Drainas, C.; Kinghorn, J.R.; Pateman, J.A. Aspartic Hydroxamate Resistance and Asparaginase Regulation in the Fungus Aspergillus nidulans. J. General Microbiol. 1977, 98, 493–501.
  • Imada, A.; Igarasi, S.; Nakahama, K.; Isono, M. Asparaginase and Glutaminase Activities of micro-organisms. J. Gen. Microbiol. 1973, 76, 85–99.
  • Charney, J.; Tomarelli, R.M. A Colorimetric Method for the Determination of the Proteolytic Activity of Duodenal Juice. J. Biol. Chem 1947, 170, 501–505.
  • Bradford, M.A. Rapid and Sensitive Method for the Quantification of Microgram Quanties of Protein Utilizing the Principle of Protein Dye Binding. Anal. Biochem. 1976, 72, 248–254.
  • Augusto, E.F.P.; Moraes, A.M.; Piccoli, R.A.M.; Barral, M.F.; Suazo, C.A.T.; Tonso, A.; Pereira, C.A. Nomenclature and Guideline to Express the Amount of a Membrane Protein Synthesized in Animal Cells in View of Bioprocess Optimization and Production Monitoring. Biologicals 2010, 38, 105–112.
  • Hiss, H. Cinética de Processos Fermentativos. In Biotecnologia Industrial: Volume 2 - Engenharia Bioquímica, Schimidell, W., Lima, U.A., Aquarone, E., e Borzani, W., Eds., 2nd ed; Edgard Blücher ltda., São Paulo, 2001; pp. 93–122.
  • Verma, N.; Kumar, K.; Kaur, G.; Anand, S. L-Asparaginase: A Promising Chemotherapeutic Agent. Crit. Rev. Biotechnol. 2007, 27, 45–62.
  • Kotzia, G.A.; Labrou, N.E. Cloning, Expression and Characterisation of Erwinia carotovora L-Asparaginase. J. Biotechnol. 2005, 119, 309–323.
  • Khushoo, A.; Pal, Y.; Singh, B.N.; Mukherjee, K.J. Extracellular Expression and Single Step Purification of Recombinant Escherichia coli L-Asparaginase II. Protein Expr. Purif. 2004, 38, 29–36.
  • Rajesh, M.J.; Rajesh, L.; Veni, V.V.S.; Thirumurugan, T.; Sivasubramanian, R.M. Effect of Inducers and Physical Parameters on the Production of L-Asparaginase Using Aspergillus terreus. J Bioproces Biotech 2011, 1, 1–6.
  • Baskar, G.; Renganatha, S. Optimization of Media Components and Operating Conditions for Exogenous Production of Fungal L-Asparaginase. Chiang Mai J. Sci. 2011, 38, 270–279.
  • Dunlop, P.C.; Roon, R.B. L-Asparaginase of Saccharomyces cerevisiae: An Extracellular Enzyme. J. Bacteriol. 1975, 1, 1017–1024.
  • Paul, J.; Cooksey, K.E. Regulation of Asparaginase, Glutamine Synthetase, and Glutamate Dehydrogenase in Response to Medium Nitrogen Concentrations in a Euryhaline Chiamydomonas Species. Plant Physiol. 1981, 68, 1364–1368.
  • Narayana, K.J.P.; Kumar, K.G.; Vijayalakshmi, M. L-Asparaginase Production by Streptomyces albidoflavus. Indian J. Microbiol. 2008, 48, 331–336.
  • Geckil, H.; Gencer, S.; Ates, B.; Ozer, U.; Uckun, M.; Yilmaz, I. Effect of Vitreoscilla Hemoglobin on Production of a Chemotherapeutic Enzyme, L-Asparaginase, by Pseudomonas aeruginosa. Biotechnol. J. 2006, 1, 203–208.
  • Jennings, M.P.; Beacham, I.R. Analysis of the Escherichia coli Gene Encoding L-Asparaginase II, ansB, and Its Regulation by Cyclic AMP Receptor and FNR Proteins. J. Bacteriol. 1990, 172, 1491–1498.
  • El-Hefnawy, M.A.A.; Attia, M.; El-Hofy, M.E.; Ali, S.M.A. Optimization Production of L-Asparaginase by Locally Isolated Filamentous Fungi from Egypt. Curr. Sci. Int. 2015, 4, 330–341.
  • Uzma, F.; Murthy, K.N.; Srinivas, C. Optimization of Physiological Conditions for L-Asparaginase Production by Endophytic Fungi (Fusarium solani) Isolated from Tinospora cordifolia (Willd.) Hook. F & Thomson. Eur. J. Exp. Biol. 2016, 6, 37–45.
  • Dias, F.F.G.; Sato, H.H. Sequential Optimization Strategy for Maximum L-Asparaginase Production from Aspergillus oryzae CCT 3940. Biocatal. Agric. Biotech. 2016, 6, 33–39.
  • El-Refai, H.A.; El-Shafei, M.S.; Mostafa, H.; El-Refai, A-M.H.; El-Beih, F.M.; Awad, G.E.A.; Easa, S.M.; Gomaa, S.K. Statistical Optimization of Anti-Leukemic Enzyme L-Asparaginase Production by Penicillium cyclopium. Curr. Trends Biotech. Pharm. 2014, 8, 130–142.

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:

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:

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.