The effects of the chemical modification on immobilized lipase features are affected by the enzyme crowding in the support

• Published in: Biotechnology Progress
• Main Authors: Abellanas-Pérez, Pedro, Carballares, Diego, Rocha-Martín, Javier, Fernández-Lafuente, Roberto
• Other Authors: Agencia Estatal de Investigación (España)
• Format: Article in Journal/Newspaper
• Language: English
• Published: John Wiley & Sons 2024
• Subjects: modulation of enzyme activity; modulation of enzyme stability; protein–protein interactions; Antarc*; Antarctica
• Online Access: http://hdl.handle.net/10261/359842; https://doi.org/10.1002/btpr.3394; https://www.scopus.com/inward/record.uri?eid=2-s2.0-85173854899&doi=10.1002%2fbtpr.3394&partnerID=40&md5=5c6c9b1c1a179995c2e0b7718db126c4

In this article, we have analyzed the interactions between enzyme crowding on a given support and its chemical modification (ethylenediamine modification via the carbodiimide route and picryl sulfonic (TNBS) modification of the primary amino groups) on the enzyme activity and stability. Lipase from Thermomyces lanuginosus (TLL) and lipase B from Candida antarctica (CALB) were immobilized on octyl-agarose beads at two very different enzyme loadings, one of them exceeding the capacity of the support, one well under this capacity. Chemical modifications of the highly loaded and lowly loaded biocatalysts gave very different results in terms of activity and stability, which could increase or decrease enzyme activity depending on the enzyme support loading. For example, both lowly loaded biocatalysts increased their activity after modification while the effect was the opposite for the highly loaded biocatalysts. Additionally, the modification with TNBS of highly loaded CALB biocatalyst increased its stability while decrease the activity. © 2023 The Authors. Biotechnology Progress published by Wiley Periodicals LLC on behalf of American Institute of Chemical Engineers. Agencia Estatal de Investigación, Grant/Award Number: PID2022-136535OB-I00 Peer reviewed