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). Thermostable Xyn11 xylanase has been used to produce a biocompatible and scalable metal-organic framework (MOF) with accessible microporous channels, suitable to be used to hydrolyze xylan over consecutive cycles (Glatz et al. 2025). Xyn11 has also been used to create a novel enzyme that possess both xylanase and feruloyl esterase activity, by engineering the Xyn11 protein scaffold to introduce an esterase active site (Muñoz-Tafalla et al. 2025).
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.
Glatz J, Cases Díaz J, Salinas-Uber J, Talens-Perales D, Polaina J, Giménez-Marqués M. Channel-Directed Enzymatic Depolymerization within a Metal-Organic Framework. ACS Appl Mater Interfaces. 2025 May 21;17(20):29729-29739.
https://pubs.acs.org/doi/10.1021/acsami.5c04137.
Muñoz-Tafalla R, Cea-Rama I, Cervantes FV, Gonzalez-Alfonso JL, Plou FJ, Polaina J, Sanz-Aparicio J, Ferrer M, Guallar V, Talens-Perales D. Embedding a feruloyl esterase active site into a thermophilic endoxylanase scaffold for the degradation of feruloylated xylans. Comput Struct Biotechnol J. 2025 Sep 3;27:3814-3823.
https://www.csbj.org/article/S2001-0370(25)00363-0/fulltext
