4.6 Article

Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications

Journal

PROCESSES
Volume 10, Issue 3, Pages -

Publisher

MDPI
DOI: 10.3390/pr10030494

Keywords

immobilization; enzymes; multienzymes; microfluidic; pectinase; rhamnopyranosidase

Funding

  1. FCT-FOUNDATION FOR SCIENCE AND TECHNOLOGY, I.P., through National Funds [UID/DTP/04138/2021, UID/BIO/04565/2020]

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Enzymes are important catalysts with high specificity and catalytic activity. Immobilization of enzymes in industrial processes overcomes the limitations and enhances stability and product yield.
Enzymes are outstanding (bio)catalysts, not solely on account of their ability to increase reaction rates by up to several orders of magnitude but also for the high degree of substrate specificity, regiospecificity and stereospecificity. The use and development of enzymes as robust biocatalysts is one of the main challenges in biotechnology. However, despite the high specificities and turnover of enzymes, there are also drawbacks. At the industrial level, these drawbacks are typically overcome by resorting to immobilized enzymes to enhance stability. Immobilization of biocatalysts allows their reuse, increases stability, facilitates process control, eases product recovery, and enhances product yield and quality. This is especially important for expensive enzymes, for those obtained in low fermentation yield and with relatively low activity. This review provides an integrated perspective on (multi)enzyme immobilization that abridges a critical evaluation of immobilization methods and carriers, biocatalyst metrics, impact of key carrier features on biocatalyst performance, trends towards miniaturization and detailed illustrative examples that are representative of biocatalytic applications promoting sustainability.

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