ArticleApplied microbiology and biotechnology2021
Directed evolution of glycosyltransferase for enhanced efficiency of avermectin glucosylation.
Article in Applied microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 8 citations in OpenAlex.
- Review
- Directed evolution of a cyclodipeptide synthase with new activitiesChemical science · 2022Article
- A Star Polyamine-Based Nanocarrier Delivery System for Enhanced Avermectin Contact and Stomach Toxicity against Green Peach Aphids.Nanomaterials (Basel, Switzerland) · 2022Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Avermectin, produced by Streptomyces avermitilis, is an active compound protective against nematodes, insects, and mites. However, its potential usage is limited by its low aqueous solubility. The uridine diphosphate (UDP)-glycosyltransferase (BLC) from Bacillus licheniformis synthesizes avermectin glycosides with improved water solubility and in vitro antinematodal activity. However, enzymatic glycosylation of avermectin by BLC is limited due to the low conversion rate of this reaction. Thus, improving BLC enzyme activity is necessary for mass production of avermectin glycosides for field application. In this study, the catalytic activity of BLC toward avermectin was enhanced via directed evolution. Three mutants from the BLC mutant library (R57H, V227A, and D252V) had specific glucosylation activity for avermectin 2.0-, 1.8-, and 1.5-fold higher, respectively, than wild-type BLC. Generation of combined mutations via site-directed mutagenesis led to even further enhancement of activity. The triple mutant, R57H/V227A/D252V, had the highest activity, 2.8-fold higher than that of wild-type BLC. The catalytic efficiencies (K
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