ArticleFrontiers in bioengineering and biotechnology2020
Immobilization of the Highly Active UDP-Glucose Pyrophosphorylase From
Article in Frontiers in bioengineering and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- A modular, reusable biocatalytic flow system for UDP-GlcNAc production.Reaction chemistry & engineering · 2025Article
- Biocatalytic Approaches to Building Blocks for Enzymatic and Chemical Glycan Synthesis.JACS Au · 2023Review
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Authors and funding
9 authors.
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Abstract
Biocatalysis that produces economically interesting compounds can be carried out by using free enzymes or microbial cells. However, often the cell metabolism does not allow the overproduction or secretion of activated sugars and thus downstream processing of these sugars is complicated. Here enzyme immobilization comes into focus in order to stabilize the enzyme as well as to make the overall process economically feasible. Besides a robust immobilization method, a highly active and stable enzyme is needed to efficiently produce the product of choice. Herein, we report on the identification, gene expression, biochemical characterization as well as immobilization of the uridine-5'-diphosphate-glucose (UDP-glucose) pyrophosphorylase originating from the thermostable soil actinobacterium
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