PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2016 | 65 | 1 |

Tytuł artykułu

Characterization and optimization of biosynthesis of bioactive secondary metabolites produced by Streptomyces sp. 8812

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The nutritional requirements and environmental conditions for a submerged culture of Streptomyces sp. 8812 were determined. Batch and fed-batch Streptomyces sp. 8812 fermentations were conducted to obtain high activity of secondary metabolites. In the study several factors were examined for their influence on the biosynthesis of the active metabolites-7-hydroxy-6-oxo-2,3,4,6-tetrahydroisoquinoline-3-carboxyl acid (C₁₀H₉NO₄) and N-acetyl-3,4-dihydroxy-l-phenylalanine (C₁₁H₁₃NO₅): changes in medium composition, pH of production medium, various growth phases of seed culture, amino acid supplementation and addition of anion exchange resin to the submerged culture. Biological activities of secondary metabolites were examined with the use of dd-carboxypeptidase 64–575 and horseradish peroxidase. Streptomyces sp. 8812 mycelium was evaluated under fluorescent microscopy and respiratory activity of the strain was analyzed. Moreover, the enzymatic profiles of the strain with the use of Api®ZYM test were analyzed and genetic analysis made. Phylogenetic analysis of Streptomyces sp. 8812 revealed that its closest relative is Streptomyces capoamus JCM 4734 (98%), whereas sequence analysis for 16S rRNA gene using NCBI BLAST algorithm showed 100% homology between these two strains. Biosynthetic processes, mycelium growth and enzyme inhibitory activities of these two strains were also compared.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

65

Numer

1

Opis fizyczny

p.51-61,fig.,ref.

Twórcy

autor
  • National Institute of Public Health - National Institute of Hygiene, Warsaw, Poland
autor
  • National Institute of Public Health - National Institute of Hygiene, Warsaw, Poland
autor
  • National Institute of Public Health - National Institute of Hygiene, Warsaw, Poland
autor
  • National Institute of Public Health - National Institute of Hygiene, Warsaw, Poland
autor
  • National Institute of Public Health - National Institute of Hygiene, Warsaw, Poland
autor
  • National Institute of Public Health - National Institute of Hygiene, Warsaw, Poland
autor
  • National Institute of Public Health - National Institute of Hygiene, Warsaw, Poland

Bibliografia

  • Adam M., C. Damblon, M. Jamin, W. Zorzi, V. Dusart, M. Galleni, A. el Kharroubi, G. Piras, B.G. Spratt and W. Keck. 1991. Acyltransferase activities of the high-molecular-mass essential penicillin-binding proteins. Biochem. J. 279(Pt 2): 601–604.
  • Adam M., C. Damblon, B. Plaitin, L. Christiaens and J.M. Frére. 1990. Chromogenic depsipeptide substrates for beta-lactamases and penicillin-sensitive dd-peptidases. Biochem. J. 270(2): 525–529.
  • Arai T. and Y. Mikami. 1972. Chromogenicity of Streptomyces. Appl. Microbiol. 23(2): 402–406.
  • BD Biosciences. 2006. BD Bionutrients™ Technical Manual. Third Edition Revised, pp. 28, 42 and 52. https://www.bd.com/ds/technicalCenter/misc/br_3_2547.pdf, 2015.06.03
  • Casey J.T., P.K. Walsh and D.G. O’Shea. 2007. Characterisation of adsorbent resins for the recovery of geldanamycin from fermentation broth. Sep. Purif. Technol. 53(3): 281–288.
  • Chance B. and A.C. Maehly. 1955. Assay of Catalases and Peroxidases. Meth. Enzymol. 2:764–775.
  • Chen X.S., S. Li, L.J. Liao, X.D. Ren, F. Li, L. Tang, J.H. Zhang and Z.G. Mao. 2011. Production of ε-poly-l-lysine using a novel two-stage pH control strategy by Streptomyces sp. M-Z18 from glycerol. Bioprocess Biosyst. Eng. 34(5): 561–567.
  • Coenye T., E. Falsen, M. Vancanneyt, B. Hoste, J.R. Govan, K. Kersters and P. Vandamme. 1999. Classification of Alcaligenes faecalis-like isolates from the environment and human clinical samples as Ralstonia gilardii sp. nov. Int. J. Syst. Bacteriol. 49(2): 405–413.
  • De Azeredo L.A., M.B. De Lima, R.R. Coelho and D.M. Freire. 2006. A low-cost fermentation medium for thermophilic protease production by Streptomyces sp. 594 using feather meal and corn steep liquor. Curr. Microbiol. 53(4): 335–339.
  • Denser Pamboukian C.R., L.M. Guimaraes and M.C.R. Facciotti. 2002. Applications of image analysis in the characterization of Streptomyces olindensis in submerged culture. Braz. J. Microbiol. 33(1): 17–21.
  • Desai R.P., T. Leaf, E. Woo and P. Licari. 2002. Enhanced production of heterologous macrolide aglycones by fed-batch cultivation of Streptomyces coelicolor. J. Ind. Microbiol. Biotechnol. 28(5): 297–301.
  • Edwards U., T. Rogall, H. Blocker, M. Emde and E.C. Bottger. 1989. Isolation and direct complete nucleotide determination of entire genes. Characterization of a gene coding for 16S ribosomal RNA. Nucleic Acids Res. 17(19): 7843–7853.
  • Frère J.M., M. Leyh-Bouille, J.M. Ghuysen, M. Nieto and H.R. Perkins. 1976. Exocellular dd-carboxypeptidases-transpeptidases from Streptomyces. Methods Enzymol. 45:610–636.
  • Genilloud O., I. Gonzalez, O. Salazar, J. Martin, J.R. Tormo and F. Vicente. 2011. Current approaches to exploit actinomycetes as a source of novel natural products. J. Ind. Microbiol. Biotechnol. 38(3): 375–389.
  • Goncalves da L.O., M.F. Delle, I.L. D’Albuquerque and G.B. Marini Bettolo. 1968. The identification of ciclacidine an antibiotic from Streptomyces capoamus sp. nov. Tetrahedron. Lett. 4: 471–473.
  • Hayakawa Y., T. Iwakiri, K. Imamura, H. Seto and N. Otake. 1985. Studies on the isotetracenone antibiotics. I. Capoamycin, a new antitumor antibiotic. J. Antibiot. (Tokyo) 38(7): 957–959.
  • Hopwood D.A. 2007. Streptomyces in nature and medicine. The antibiotic makers. Oxford University Press, New York.
  • Jia B., Z.H. Jin, Y.L. Lei, L.H. Mei and N.H. Li. 2006. Improved production of pristinamycin coupled with an adsorbent resin in fermentation by Streptomyces pristinaespiralis. Biotechnol. Lett. 28(22): 1811–1815.
  • Kegg Pathway Maps. 2014. Isoquinoline alkaloid biosynthesis. http:// www.genome. jp/kegg-bin/show_pathway?map00950, 2015.06.03.
  • Keller and Heckmann LPP. 2006. Assessment Plan for Corn Steep Liquor (CAS #66071-94-1) in Accordance with the USEPA High Production Volume Chemical Challenge Program. http://www.epa. gov/HPV/pubs/summaries/cornstlq/C16469tp.pdf, 2015.06.03.
  • Lee J.C., H.R. Park, D.J. Park, H.B. Lee, Y.B. Kim and C.J. Kim. 2003. Improved production of teicoplanin using adsorbent resin in fermentations. Lett. Appl. Microbiol. 37(3):196–200.
  • Lehmann H.P., K.H. Schosinsky and M.F. Beeler. 1974. Standardization of serum ceruloplasmin concentrations in international enzyme units with o-dianisidine dihydrochloride as substrate. Clin. Chem. 20(12): 1564–1567.
  • Liao X., L.C. Vining and J.L. Doull. 1995. Physiological control of trophophase-idiophase separation in streptomycete cultures producing secondary metabolites. Can. J. Microbiol. 41(4–5): 309–315.
  • Ortiz S.C.A., C.O. Hokka and A.C. Badino. 2007. Utilization of soybean derivatives on clavulanic acid production by Streptomyces clavuligerus. Enzyme Microb Technol. 40(5): 1071–1077.
  • R Foundation for Statistical Computing. 2013. A language and environment for statistical computing. http://www.r-project org/, 2015.06.03.
  • Shirling E.B. and D. Gottlieb. 1966. Methods for characterization of Streptomyces species. Int. J. Syst. Bacteriol. 16(3): 313–340.
  • Singh V., C.K.M. Tripathi and V. Bihari. 2008. Production, optimization and purification of an antifungal compound from Streptomyces capoamus MTCC 8123. Med. Chem. Res. 17(2–7): 94–102.
  • Solecka J. and W. Kurzątkowski. 1999. Affinity of exocellular DD-carboxypeptidase/transpeptidase from Saccharopolyspora erythraea PZH TZ 64–575 to beta-lactam compounds (in Polish). Med. Dośw. Mikrobiol. 51: 151–165.
  • Solecka J., R. Lysek, B. Furman, M. Chmielewski and W. Kurzatkowski. 2003. Practical use of dd-peptidase 64–575 for the assay of inhibition activity of natural and synthetic beta-lactam compounds. Acta Pol. Pharm. 60(2): 115–118.
  • Solecka J., A. Rajnisz and A.E. Laudy. 2009a. A novel isoquinoline alkaloid, dd-carboxypeptidase inhibitor, with antibacterial activity isolated from Streptomyces sp. 8812. Part I: Taxonomy, fermentation, isolation and biological activities. J. Antibiot. (Tokyo) 62(10): 575–580.
  • Solecka J., J. Sitkowski, W. Bocian, E. Bednarek, R. Kawecki and L. Kozerski. 2009b. A novel isoquinoline alkaloid, dd-carboxypeptidase inhibitor, with antibacterial activity isolated from Streptomyces sp. 8812. Part II: Physicochemical properties and structure elucidation. J. Antibiot. (Tokyo) 62(10): 581–585.
  • Solecka J., A. Rajnisz, M. Postek, J. Zajko, R. Kawecki, V. Havlicek, E. Bednarek and L. Kozerski. 2012a. N-acetyl-3,4-dihydroxy-l-phenylalanine, a second identified bioactive metabolite produced by Streptomyces sp. 8812. J. Antibiot. (Tokyo) 65(4): 219–221.
  • Solecka J., J. Zajko, A. Rajnisz and M.A. Postek. 2012b. Searching for novel, bioactive compounds derived from nature (in Polish). Gaz. Farmaceutyczna 1:36–38.
  • Tsueng G. and K.S. Lam. 2007. Stabilization effect of resin on the production of potent proteasome inhibitor NPI-0052 during submerged fermentation of Salinispora tropica. J. Antibiot. (Tokyo) 60(7): 469–472.
  • Zhang L.J., Z.H. Jin, X.G. Chen, Q.C. Jin, and M.G. Feng. 2012. Glycine feeding improves pristinamycin production during fermentation including resin for in situ separation. Bioprocess Biosyst. Eng. 35(4): 513–517.
  • Zhinan X. and C. Peilin. 1999. Enhanced production of avermectin B1a by medium optimization and glucose feeding with Streptomyces avermilitis. Bioprocess Biosyst. Eng. 20(1): 67–71.
  • Zou X., H.F. Hang, J. Chu, Y.P. Zhuang, and S.L. Zhang. 2009. Oxygen uptake rate optimization with nitrogen regulation for erythromycin production and scale-up from 50 l to 372 m3 scale. Bioresour. Technol. 100(3): 1406–1412.
  • Zou X., W.J. Li, W. Zeng, J. Chu, Y.P. Zhuang and S.L. Zhang. 2011. An assessment of seed quality on erythromycin production by recombinant Saccharopolyspora erythraea strain. Bioresour. Technol. 102(3): 3360–3365.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-8ba4c322-d38f-4d1b-8fe2-5b55c4028617
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.