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Development of stable enzymes has been identified as a key requirement for future application of UDP-glycosyltransferases as biocatalysts. To the best of our knowledge, no thermostable or pH tolerant UGT has been reported. Instead, we will draw on a vast amount of studies done on other types of enzymes. For example, stabilization of flexible sites through introduction of salt or disulphide bridges has been useful. Since the GT-B fold of UDP-glycosyltransferases contains many flexible loops of varying length, this is an obvious strategy to pursue, along with random mutagenesis and directed evolution.
StatusCurrent
Period01/04/201831/03/2020
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ID: 150478476