"One Gene - One Enzyme - One NewCo"

Research

 We study the structure and function of enzymes with potential biotechnological applications. To this end we use a multidisciplinary approach that includes structural analysis, to solve the protein three-dimensional structure; random and rationally driven gene mutation, to modify enzyme properties; in silico mining of enzyme with specific properties from protein sequence databases. Enzymes with selected properties can be used as such or incorporated into zymoactive materials or genetically modified organisms.

Some of our research projects

Xylanases

Plant biomass is used as raw material in many processes, such as paper manufacturing and ethanol production. However, it is also a waste product derived from agri-food activities, currently posing a significant environmental problem. Utilizing this biomass is one of the challenges we face as a society to meet sustainable development goals, which align with the concept of a circular economy.

Xylanases are among the most widely used enzymes for processing plant biomass. However, their use is limited due to low performance under the extreme conditions required by industry. Therefore, the search for xylanases capable of functioning in such conditions is a relevant goal. A comprehensive analysis using bioinformatic methods allowed their classification, structural analysis, and identification of groups of thermophilic and alkalophilic xylanase sequences for laboratory testing.

The characterized xylanases hydrolyzed xylan with high efficiency, particularly Xyn11, which exhibited activity at pH 10.5 and 90°C—extreme conditions suitable for industrial processes. This study represents a productive approach for selecting suitable enzymes using the information contained in extensive databases (Talens-Perales et al., 2020, Talens-Perales et al., 2022, Almeida et al., 2022, Cabrera-Villamizar et al., 2024).

References

Talens-Perales, D., Jiménez-Ortega, E., Sánchez-Torres, P., Sanz-Aparicio, J., & Polaina, J. (2021). Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity. Computational and Structural Biotechnology Journal. Elsevier BV. http://doi.org/10.1016/j.csbj.2021.05.004.

Talens-Perales, D., Sánchez-Torres, P., Marín-Navarro, J., & Polaina, J. (2020, December). In silico screening and experimental analysis of family GH11 xylanases for applications under conditions of alkaline pH and high temperature. Biotechnology for Biofuels. Springer Science and Business Media LLC. http://doi.org/10.1186/s13068-020-01842-5.

Almeida, N., Meyer, V., Burnet, A., Boucher, J., Talens-Perales, D., Pereira, S., Ihalainen, P., Levée, T., Polaina J., Petit-Conil, M., Camarero, S. Pinto, P. (2022, November 3). Use of a Novel Extremophilic Xylanase for an Environmentally Friendly Industrial Bleaching of Kraft Pulps. International Journal of Molecular Sciences. MDPI AG. http://doi.org/10.3390/ijms232113423.

Cabrera-Villamizar, L. A., Ebrahimi, M., Martínez-Abad, A., Talens-Perales, D., López-Rubio, A., & Fabra, M. J. (2024, March). Order matters: Methods for extracting cellulose from rice straw by coupling alkaline, ozone and enzymatic treatments. Carbohydrate Polymers. Elsevier BV. http://doi.org/10.1016/j.carbpol.2023.121746.

Collaborators

Enzymatics
Enzymology
Enzymatics
Enzymology