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Enhancing the Thermostability of Glucose Isomerase by Protein Engineering

Bio/Technology volume 9, pages 738–742 (1991)Cite this article

Abstract

We have engineered recombinant glucose isomerase (GI) from Actinoplanes missouriensis by site-directed mutagenesis to enhance its thermal stability in both the soluble and immobilized forms. Substitution of arginine for lysine at position 253, which lies at the dimer/dimer interface of the GI tetramer, produced the largest stabilization under model industrial conditions. We discuss our results in terms of a model in which chemical glycation of lysines by sugars in the industrial corn syrup substrate represents a major pathway of destabilization.

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Author notes

  1. Nadir T. Mrabet

    Present address: Université Libre de Bruxelles, Unité Conformation des Macromolécules Biologiques, Avenue Paul Heger, B1050, Brussels, Belgium

  2. Wim J. Quax and Nadir T. Mrabet: Corresponding authors.

Authors and Affiliations

  1. Gist-brocades, Research & Development, Wateringseweg 1, 2611 XT, Delft, The Netherlands

    Wim J. Quax, Ruud G. M. Luiten & Paul W. Schuurhuizen

  2. Plant Genetic Systems, Protein Engineering Dept., 22 Jozef Plateau Straat, B-9000, Gent, Belgium

    Nadir T. Mrabet, Patrick Stanssens & Ignace Lasters

Authors
  1. Wim J. Quax
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  2. Nadir T. Mrabet
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  3. Ruud G. M. Luiten
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  4. Paul W. Schuurhuizen
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  5. Patrick Stanssens
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  6. Ignace Lasters
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Quax, W., Mrabet, N., Luiten, R. et al. Enhancing the Thermostability of Glucose Isomerase by Protein Engineering. Nat Biotechnol 9, 738–742 (1991). https://doi.org/10.1038/nbt0891-738

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