Joaquín Moreno Biochemistry and Molecular Biology, University of Valencia, Spain
2 protocols

Lola Peñarrubia Biochemistry and Molecular Biology, University of Valencia, Spain
2 protocols

Carlos García-Ferris Biochemistry and Molecular Biology, University of Valencia, Spain
2 protocols

María García-Murria Biochemistry and Molecular Biology, University of Valencia, Spain
2 protocols

Julia Marín-Navarro
  • Biochemistry and Molecular Biology, University of Valencia, Spain
Research focus
  • Plant science
  • 2 Author merit


Ph.D. in Biochemistry, Department of Biochemistry, University of Valencia, Spain, 2004

Current position

Researcher at Institute of Agricultural Chemistry and Food Technology (IATA-CSIC), Spain
Associate professor at Department of Biochemistry and Molecular Biology, University of Valencia, Spain

Publications (since 2005)

  1. Marin-Navarro, J., Talens-Perales, D. and Polaina, J. (2015). One-pot production of fructooligosaccharides by a Saccharomyces cerevisiae strain expressing an engineered invertase. Appl Microbiol Biotechnol 99(6): 2549-2555.
  2. Marin-Navarro, J., Talens-Perales, D., Oude-Vrielink, A., Canada, F. J. and Polaina, J. (2014). Immobilization of thermostable beta-galactosidase on epoxy support and its use for lactose hydrolysis and galactooligosaccharides biosynthesis. World J Microbiol Biotechnol 30(3): 989-998.
  3. Sainz-Polo, M. A., Ramirez-Escudero, M., Lafraya, A., Gonzalez, B., Marin-Navarro, J., Polaina, J. and Sanz-Aparicio, J. (2013). Three-dimensional structure of Saccharomyces invertase: role of a non-catalytic domain in oligomerization and substrate specificity. J Biol Chem 288(14): 9755-9766.
  4. Ferrer, M., Ghazi, A., Beloqui, A., Vieites, J. M., Lopez-Cortes, N., Marin-Navarro, J., Nechitaylo, T. Y., Guazzaroni, M. E., Polaina, J., Waliczek, A., Chernikova, T. N., Reva, O. N., Golyshina, O. V. and Golyshin, P. N. (2012). Functional metagenomics unveils a multifunctional glycosyl hydrolase from the family 43 catalysing the breakdown of plant polymers in the calf rumen. PLoS One 7(6): e38134.
  5. Sainz-Polo, M. A., Lafraya, A., Polo, A., Marin-Navarro, J., Polaina, J. and Sanz-Aparicio, J. (2012). Crystallization and preliminary X-ray diffraction analysis of the invertase from Saccharomyces cerevisiae. Acta Crystallogr Sect F Struct Biol Cryst Commun 68(Pt 12): 1538-1541.
  6. Marin-Navarro, J. and Polaina, J. (2011). Glucoamylases: structural and biotechnological aspects. Appl Microbiol Biotechnol 89(5): 1267-1273.
  7. Marin-Navarro, J., Gurgu, L., Alamar, S. and Polaina, J. (2011). Structural and functional analysis of hybrid enzymes generated by domain shuffling between Saccharomyces cerevisiae (var. diastaticus) Sta1 glucoamylase and Saccharomycopsis fibuligera Bgl1 beta-glucosidase. Appl Microbiol Biotechnol 89(1): 121-130.
  8. Marin-Navarro, J., Jauhiainen, A., Moreno, J., Alepuz, P., Perez-Ortin, J. E. and Sunnerhagen, P. (2011). Global estimation of mRNA stability in yeast. Methods Mol Biol 734: 3-23.
  9. Gurgu, L., Lafraya, A., Polaina, J. and Marin-Navarro, J. (2011). Fermentation of cellobiose to ethanol by industrial Saccharomyces strains carrying the beta-glucosidase gene (BGL1) from Saccharomycopsis fibuligera. Bioresour Technol 102(8): 5229-5236.
  10. Lafraya, A., Sanz-Aparicio, J., Polaina, J. and Marin-Navarro, J. (2011). Fructo-oligosaccharide synthesis by mutant versions of Saccharomyces cerevisiae invertase. Appl Environ Microbiol 77(17): 6148-6157.
  11. Marín‐Navarro, J., García‐Murria, M. J. and Moreno, J. (2010). REDOX PROPERTIES ARE CONSERVED IN RUBISCOS FROM DIATOMS AND GREEN ALGAE THROUGH A DIFFERENT PATTERN OF CYSTEINES1. Journal of Phycology 46(3): 516-524.
  12. Marín-Navarro, J., Esquivel, M. G. and Moreno, J. (2010). Hydrogen production by Chlamydomonas reinhardtii revisited: Rubisco as a biotechnological target. World Journal of Microbiology and Biotechnology 26(10): 1785-1793.
  13. Moreno, J., Garcia-Murria, M. J. and Marin-Navarro, J. (2008). Redox modulation of Rubisco conformation and activity through its cysteine residues. J Exp Bot 59(7): 1605-1614.
  14. Garcia-Murria, M. J., Karkehabadi, S., Marin-Navarro, J., Satagopan, S., Andersson, I., Spreitzer, R. J. and Moreno, J. (2008). Structural and functional consequences of the replacement of proximal residues Cys(172) and Cys(192) in the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from Chlamydomonas reinhardtii. Biochem J 411(2): 241-247.
  15. Molina-Navarro, M. M., Castells-Roca, L., Belli, G., Garcia-Martinez, J., Marin-Navarro, J., Moreno, J., Perez-Ortin, J. E. and Herrero, E. (2008). Comprehensive transcriptional analysis of the oxidative response in yeast. J Biol Chem 283(26): 17908-17918.
  16. Mayfield, S. P., Manuell, A. L., Chen, S., Wu, J., Tran, M., Siefker, D., Muto, M. and Marin-Navarro, J. (2007). Chlamydomonas reinhardtii chloroplasts as protein factories. Curr Opin Biotechnol 18(2): 126-133.
  17. Marin-Navarro, J., Manuell, A. L., Wu, J. and S, P. M. (2007). Chloroplast translation regulation. Photosynth Res 94(2-3): 359-374.
  18. Esquivel, M. G., Pinto, T. S., Marin-Navarro, J. and Moreno, J. (2006). Substitution of tyrosine residues at the aromatic cluster around the betaA-betaB loop of rubisco small subunit affects the structural stability of the enzyme and the in vivo degradation under stress conditions. Biochemistry 45(18): 5745-5753.
  19. Marin-Navarro, J. and Moreno, J. (2006). Cysteines 449 and 459 modulate the reduction-oxidation conformational changes of ribulose 1.5-bisphosphate carboxylase/oxygenase and the translocation of the enzyme to membranes during stress. Plant Cell Environ 29(5): 898-908.
2 Protocols published
Chlamydomonas reinhardtii is a model organism for chloroplast studies. Besides other convenient features, the feasibility of chloroplast genome transformation distinguishes this unicellular alga as ideal for the manipulation of ...
The performance of the carbon-fixing enzyme, ribulose 1, 5-bisphosphate carboxylase/oxygenase (EC, Rubisco), controls biomass accumulation in green plants, algae and most autotrophic bacteria. In particular, the carboxylase activity of ...
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