ArticleApplied microbiology and biotechnology2021
Development of thermostable sucrose phosphorylase by semi-rational design for efficient biosynthesis of alpha-D-glucosylglycerol.
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 19 papers, 1 of them a synthesis that pooled it.
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Who cites it
19 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.
- Computer-Aided Lipase Engineering for Improving Their Stability and Activity in the Food Industry: State of the Art.Molecules (Basel, Switzerland) · 2023Pooled it
- Improved biosynthesis of lactulose by a novel thermostable cellobiose-2-epimerase generated through semi-rational mutagenesis.World journal of microbiology & biotechnology · 2025Article
- Article
- Codeine 3-O-demethylase catalyzed biotransformation of morphinan alkaloids in Escherichia coli: site directed mutagenesis of terminal residues improves enzyme expression, stability and biotransformation yield.Journal of biological engineering · 2025Article
- Enzymes for Biomass Pretreatment: A Comprehensive Review.Advances in biochemical engineering/biotechnology · 2025Review
- A general temperature-guided language model to design proteins of enhanced stability and activity.Science advances · 2024Article
- 2-O-α-D-glucosyl glycerol production by whole-cell biocatalyst of lactobacilli encapsulating sucrose phosphorylase with improved glycerol affinity and conversion rate.Microbial cell factories · 2024Article
- Advancements in the Heterologous Expression of Sucrose Phosphorylase and Its Molecular Modification for the Synthesis of Glycosylated Products.Molecules (Basel, Switzerland) · 2024Review
- Functional expression, purification, biochemical and biophysical characterizations, and molecular dynamics simulation of a histidine acid phosphatase from Saccharomyces cerevisiae.World journal of microbiology & biotechnology · 2024Article
- A Bibliometric Analysis: Current Perspectives and Potential Trends of Enzyme Thermostability from 1991-2022.Applied biochemistry and biotechnology · 2024Article
- Characterization of a novel sucrose phosphorylase from Paenibacillus elgii and its use in biosynthesis of α-arbutin.World journal of microbiology & biotechnology · 2023Article
- Energy- and evolution-based design of inulosucrase for enhanced thermostability and inulin production.Applied microbiology and biotechnology · 2023Article
- Research progress and application of enzymatic synthesis of glycosyl compounds.Applied microbiology and biotechnology · 2023Review
- Combinatorial metabolic engineering enables high yield production of α-arbutin from sucrose by biocatalysis.Applied microbiology and biotechnology · 2023Article
- Efficient Production of 2-O-α-D-Glucosyl Glycerol Catalyzed by an Engineered Sucrose Phosphorylase from Bifidobacterium longum.Applied biochemistry and biotechnology · 2022Article
- Expanding the Substrate Scope of a Bacterial Nucleotidyltransferase via Allosteric Mutations.ACS infectious diseases · 2022Article
- Thermostability engineering of industrial enzymes through structure modification.Applied microbiology and biotechnology · 2022Review
- Making Enzymes Suitable for Organic Chemistry by Rational Protein Design.Chembiochem : a European journal of chemical biology · 2022Review
- Improving Thermostability and Catalytic Activity of Glycosyltransferase FromFrontiers in bioengineering and biotechnology · 2022Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
Abstract
Sucrose phosphorylase (SPase) can specifically catalyze transglycosylation reactions and can be used to enzymatically synthesize α-D-glycosides. However, the low thermostability of SPase has been a bottleneck for its industrial application. In this study, a SPase gene from Leuconostoc mesenteroides ATCC 12,291 (LmSPase) was synthesized with optimized codons and overexpressed successfully in Escherichia coli. A semi-rational design strategy that combined the FireProt (a web server designing thermostable proteins), structure-function analysis, and molecular dynamic simulations was used to improve the thermostability of LmSPase. Finally, one single-point mutation T219L and a combination mutation I31F/T219L/T263L/S360A (Mut4) with improved thermostability were obtained. The half-lives at 50 °C of T219L and Mut4 both increased approximately two-fold compared to that of wild-type LmSPase (WT). Furthermore, the two variants T219L and Mut4 were used to produce α-D-glucosylglycerol (αGG) from sucrose and glycerol by incubating with 40 U/mL crude extracts at 37 °C for 60 h and achieved the product concentration of 193.2 ± 12.9 g/L and 195.8 ± 13.1 g/L, respectively, which were approximately 1.3-fold higher than that of WT (150.4 ± 10.0 g/L). This study provides an effective strategy for improving the thermostability of an industrial enzyme. KEY POINTS: • Predicted potential hotspot residues directing the thermostability of LmSPase by semi-rational design • Screened two positive variants with higher thermostability and higher activity • Synthesized α-D-glucosylglycerol to a high level by two screened positive variants.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.