Mechanism of thermoinactivation of immobilized glucose isomerase

@article{Volkin1989MechanismOT,
  title={Mechanism of thermoinactivation of immobilized glucose isomerase},
  author={David B. Volkin and Alexander M. Klibanov},
  journal={Biotechnology and Bioengineering},
  year={1989},
  volume={33}
}
Irreversible thermoinactivation of immobilized glucose isomerase from Streptomyces olivochromogenes has been mechanistically investigated at the pH‐optimum of enzymatic activity (pH 8.0). Ligands (high fructose corn syrup and the competitive inhibitor xylitol) greatly stabilize the immobilized enzyme at high temperatures. At 90°C in the presence of 2M xylitol, irreversible inactivation of immobilized glucose isomerase is caused by deamidation of its asparagine/glutamine residues. On the basis… Expand
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Purification and characterization of a highly thermostable glucose isomerase produced by the extremely thermophilic eubacterium, Thermotoga maritima
  • Stephen H. Brown, C. Sjøholm, Robert M. Kelly
  • Biology, Medicine
  • Biotechnology and bioengineering
  • 1993
TLDR
The high degree of thermostability, coupled with a neutral to slightly acid pH optimum, reveal this enzyme to be a promising candidate for improvement of the industrial glucose isomerization process. Expand
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