Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 210, Issue -, Pages 682-702Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2022.04.224
Keywords
Multi-point covalent immobilization; Ion exchange; Glutaraldehyde versatility
Funding
- Ministerio de Ciencia e Innovacion from Spanish Government [CTQ201786170-R]
- Agencia Estatal de Investigacion [PID2021-122398OB-I00]
- CSIC [AEP045]
- FPU fellowship (Ministerio de Educacion)
- Programa para el Desarrollo Profesional Docente (PRODEP) from Mexican Government
- Ministerio de Ciencia, Innovacion y Universidades [RTI2018-095291-B-I00]
- FEDER [RTI2018-095291-B-I00]
- Generalitat Valenciana [PROMETEOII/2018/076]
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This article highlights the complexities of immobilizing pepsin and discusses potential methods and applications. The lack of primary amino groups on the enzyme's surface and its poor stability at alkaline pH values present challenges for immobilization. The review also proposes possibilities for achieving both covalent immobilization and stabilization of pepsin through multipoint covalent attachment.
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.
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