Biotechnology Letters

, Volume 29, Issue 8, pp 1227–1232 | Cite as

Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5

  • Jacob Dam Sørensen
  • Evamaria I. Petersen
  • Marilyn G. Wiebe
Original Research Paper
First Online:
Received:
Revised:
Accepted:

Abstract

Fusarium venenatum A3/5 was transformed using the Aspergillus niger expression plasmid, pIGF, in which the coding sequence for the F. solani f. sp. pisi cutinase gene had been inserted in frame, with a KEX2 cleavage site, with the truncated A. niger glucoamylase gene under control of the A. niger glucoamylase promoter. The transformant produced up to 21 U cutinase l−1 in minimal medium containing glucose or starch as the primary carbon source. Glucoamylase (165 U l−1 or 8 mg l−1) was also produced. Both the transformant and the parent strain produced cutinase in medium containing cutin.

Keywords

Cutinase Fusarium venenatum Recombinant protein 
This is a preview of subscription content, log in to check access.

Notes

Acknowledgement

This work was funded by grant no. 26-10-0159 from the Danish Technical Research Council.

References

  1. Blinkovsky AM, Byun T, Brown KM, Golightly EJ (1999) Purification, characterization, and heterologous expression in Fusarium venenatum of a novel serine carboxypeptidase from Aspergillus oryzae. Appl Environ Microbiol 65:3298–3303PubMedGoogle Scholar
  2. Gordon C, Thomas S, Griffen A, Robson GD, Trinci APJ, Wiebe MG (2001) Combined use of growth rate correlated and growth rate independent promoters for recombinant glucoamylase production in Fusarium venenatum. FEMS Microbiol Lett 194:229–234PubMedCrossRefGoogle Scholar
  3. Lauwereys M, de Geus P, de Meutter J, Stanssens P, Mathyssens G (1991) Cloning, expression and characterization of cutinase, a fungal lipolytic enzyme. In: Alberghina L, Schmid RD, Verger R (eds) Lipases-structure, function and genetic engineering. VCH, Weinheim, pp 243–251Google Scholar
  4. Lin TS, Kolattukudy PE (1978) Induction of a biopolyester hydrolase (cutinase) by low levels of cutin monomers in Fusarium solani f. sp. pisi. J Bacteriol 133:942–951PubMedGoogle Scholar
  5. Mainwaring DO, Wiebe MG, Robson GD, Goldrick M, Jeenes DJ, Archer DG, Trinci APJ (1999) Effect of pH on hen egg white lysozyme production and evolution of a recombinant strain of Aspergillus niger. J Biotechnol 75:1–10PubMedCrossRefGoogle Scholar
  6. Meyers SA, Cuppett SL, Hutkins RW (1996) Lipase production by lactic acid bacteria and activity on butter oil. Food Microbiol 13:383–389CrossRefGoogle Scholar
  7. Neves-Petersen MT, Petersen EI, Fojan P, Noronha M, Madsen RG, Petersen SB (2001) Engineering the pH-optimum of a triglyceride lipase: from predictions based on electrostatic computations to experimental results. J Biotechnol 87:225–254PubMedCrossRefGoogle Scholar
  8. Osman SF, Irwin P, Fett WF, O’Connor JV, Parris N (1999) Preparation, isolation, and characterization of cutin monomers and oligomers from tomato peels. J Agric Food Chem 47:799–802PubMedCrossRefGoogle Scholar
  9. Punt PJ, van den Hondel CAMJJ (1992) Transformation of filamentous fungi based on hygromycin B and phleomycin resistance markers. Methods Enzymol 216:447–457PubMedCrossRefGoogle Scholar
  10. Purdy RE, Kolattukudy PE (1975) Hydrolysis of plant cutin by plant pathogens. Purification, amino acids composition, and molecular weight of two isoenzymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi. Biochemistry 14:2824–2831PubMedCrossRefGoogle Scholar
  11. Royer JC, Moyer DL, Reiwitch SG, Madden MS, Jensen EB, Brown SH, Yonker CC, Johnstone JA, Golightly EJ, Yoder WT, Shuster JR (1995) Fusarium graminearum A3/5 as a novel host for heterologous protein production. Bio/Technology 13:1479–1483PubMedCrossRefGoogle Scholar
  12. Sebastian J, Chandra AK, Kolattukudy PE (1987) Discovery of a cutinase-producing Pseudomonas sp. cohabiting with an apparently nitrogen-fixing Corynebacterium sp. in phyllosphere. J Bacteriol 169:131–136PubMedGoogle Scholar
  13. van Gemeren IA, Musters W, van den Hondel CAMJJ, Verrips CT (1995) Construction and heterologous expression of a synthetic copy of the cutinase cDNA from Fusarium solani pisi. J Biotechnol 40:155–162PubMedCrossRefGoogle Scholar
  14. Verrips T, Duboc P, Visser C, Sagt C (2000) From gene to product in yeast: production of fungal cutinase. Enzyme Microb Technol 26:812–818CrossRefGoogle Scholar
  15. Vogel HJ (1956) A convenient growth medium for Neurospora (Medium N). Microbial Genet Bull 243:112–119Google Scholar
  16. Wang GY, Michailides TJ, Hammock BD, Lee Y-M, Bostock RM (2002) Molecular cloning, characterization, and expression of a redox-responsive cutinase from Monilinia fructicola (Wint) honey. Fungal Genet Biol 35:261–276PubMedCrossRefGoogle Scholar
  17. Wiebe MG, Robson GD, Shuster JR, Trinci APJ (2000) Growth rate independent production of recombinant glucoamylase by Fusarium venenatum JeRS 325. Biotechnol Bioeng 68:245–251PubMedCrossRefGoogle Scholar
  18. Wiebe MG, Robson GD, Shuster J, Trinci APJ (2001) Evolution of a recombinant (glucoamylase-prodcuing) strain of Fusarium venenatum A3/5 in chemostat culture. Biotechnol Bioeng 73:146–156PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  • Jacob Dam Sørensen
    • 1
    • 4
  • Evamaria I. Petersen
    • 2
  • Marilyn G. Wiebe
    • 1
    • 3
  1. 1.Department of Biotechnology, Chemistry and Environmental EngineeringAalborg UniversityAalborgDenmark
  2. 2.Department of Physics and NanotechnologyAalborg UniversityAalborg EastDenmark
  3. 3.VTTEspooFinland
  4. 4.Novo Nordisk A/S, Hallas AlléKalundborgDenmark

Personalised recommendations