Morellon-Sterling, RobertoTavano, OlgaBolívar Bolívar, Juan ManuelBerenguer-Murcia, ÁngelVela-Gutiérrez, GilberSabir, JamalTacias-Pascacio, VeymarFernandez-Lafuente, Roberto2024-02-202024-02-202022Morellon-Sterling, R., Tavano, O., Bolivar, J. M., Berenguer-Murcia, Á., Vela-Gutiérrez, G., Sabir, J. S. M., Tacias-Pascacio, V. G., & Fernandez-Lafuente, R. (2022). A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values [Review of A review on the immobilization of pepsin: A Lys-poor enzyme that is unstable at alkaline pH values]. International Journal of Biological Macromolecules, 210, 682-702. Elsevier B.V. https://doi.org/10.1016/J.IJBIOMAC.2022.04.2240141-813010.1016/j.ijbiomac.2022.04.224https://hdl.handle.net/20.500.14352/101578We gratefully recognize the support from the Ministerio de Ciencia e Innovación from Spanish Government (project number CTQ2017-86170-R), Agencia Estatal de Investigacion (PID2021-122398OB-I00) and CSIC for the project AEP045. The FPU fellowship (Ministerio de Educacion) for Mr. Morellon–Sterling is gratefully recognized. Dr. Tacias-Pascacio thanks the financial support from “Programa para el Desarrollo Profesional Docente” (PRODEP) from Mexican Government. ABM would like to thank Ministerio de Ciencia, Innovación y Universidades and FEDER (Project RTI2018-095291-B-I00) and the Generalitat Valenciana (PROMETEOII/2018/076) for financial support.Pepsin is a protease used in many different applications, and in many instances, it is utilized in an immobilized form to prevent contamination of the reaction product. This enzyme has two peculiarities that make its immobilization complex. The first one is related to the poor presence of primary amino groups on its surface (just one Lys and the terminal amino group). The second one is its poor stability at alkaline pH values. Both features make the immobilization of this enzyme to be considered a complicated goal, as most of the immobilization protocols utilize primary amino groups for immobilization. This review presents some of the attempts to get immobilized pepsin biocatalyst and their applications. The high density of anionic groups (Asp and Glu) make the anion exchange of the enzyme simpler, but this makes many of the strategies utilized to immobilize the enzyme (e.g., amino-glutaraldehyde supports) more related to a mixed ion exchange/hydrophobic adsorption than to real covalent immobilization. Finally, we propose some possibilities that can permit not only the covalent immobilization of this enzyme, but also their stabilization via multipoint covalent attachment.engAttribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/journal article1879-0003https://doi.org/10.1016/J.IJBIOMAC.2022.04.224open access66.0620Multi-point covalent immobilizationIon exchangeGlutaraldehyde versatilityIngeniería químicaQuímica industrialBioquímica (Química)2302 Bioquímica3302 Tecnología Bioquímica3303 Ingeniería y Tecnología Químicas