Enhancing the Thermostability of Glucose Isomerase by Protein Engineering
- 1 August 1991
- journal article
- Published by Springer Nature in Nature Biotechnology
- Vol. 9 (8) , 738-742
- https://doi.org/10.1038/nbt0891-738
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.Keywords
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