ArticleBiotechnology for biofuels2021
Improvement of thermostability and catalytic efficiency of glucoamylase from Talaromyces leycettanus JCM12802 via site-directed mutagenesis to enhance industrial saccharification applications.
Article in Biotechnology for biofuels, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed.
- Rational Design ofBiotech (Basel (Switzerland)) · 2026Article
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- Generation and characterization of two acid-resistant macrocinComputational and structural biotechnology journal · 2024Article
- Boosting Fructosyl Transferase's Thermostability and Catalytic Performance for Highly Efficient Fructooligosaccharides (FOS) Production.Foods (Basel, Switzerland) · 2024Article
- Computer-aided rational design strategy based on protein surface charge to improve the thermal stability of a novel esterase from Geobacillus jurassicus.Biotechnology letters · 2024Article
- Review
- Microbial glucoamylases: structural and functional properties and biotechnological uses.World journal of microbiology & biotechnology · 2023Review
- A high-throughput dual system to screen polyphosphate kinase mutants for efficient ATP regeneration in L-theanine biocatalysis.Biotechnology for biofuels and bioproducts · 2023Article
- The effect of barium and strontium on activity of glucoamylase QsGH97a from Qipengyuania seohaensis SW-135.Scientific reports · 2023Article
- Possibilities of Using De Novo Design for Generating Diverse Functional Food Enzymes.International journal of molecular sciences · 2023Review
- Simultaneous Improvement of Final Product-Tolerance and Thermostability of GH39 Xylosidase for Prebiotic Production by Directed Evolution.Foods (Basel, Switzerland) · 2022Article
- Identification and Mutation Analysis of Nonconserved Residues on the TIM-Barrel Surface of GH5_5 Cellulases for Catalytic Efficiency and Stability Improvement.Applied and environmental microbiology · 2022Article
- Improving the Specific Activity and Thermostability of Psychrophilic Xylosidase AX543 by Comparative Mutagenesis.Foods (Basel, Switzerland) · 2022Article
- Engineering a carbohydrate-binding module to increase the expression level of glucoamylase in Pichia pastoris.Microbial cell factories · 2022Article
- Improving Thermostability of Chimeric Enzymes Generated by Domain Shuffling Between Two Different Original Glucoamylases.Frontiers in bioengineering and biotechnology · 2022Article
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12 authors.
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Abstract
backgroundGlucoamylase is an important industrial enzyme in the saccharification of starch into glucose. However, its poor thermostability and low catalytic efficiency limit its industrial saccharification applications. Therefore, improving these properties of glucoamylase is of great significance for saccharification in the starch industry.
resultsIn this study, a novel glucoamylase-encoding gene TlGa15B from the thermophilic fungus Talaromyces leycettanus JCM12802 was cloned and expressed in Pichia pastoris. The optimal temperature and pH of recombinant TlGa15B were 65 ℃ and 4.5, respectively. TlGa15B exhibited excellent thermostability at 60 ℃. To further improve thermostability without losing catalytic efficiency, TlGa15B-GA1 and TlGa15B-GA2 were designed by introducing disulfide bonds and optimizing residual charge-charge interactions in a region distant from the catalytic center. Compared with TlGa15B, mutants showed improved optimal temperature, melting temperature, specific activity, and catalytic efficiency. The mechanism underlying these improvements was elucidated through molecular dynamics simulation and dynamics cross-correlation matrices analysis. Besides, the performance of TlGa15B-GA2 was the same as that of the commercial glucoamylase during saccharification.
conclusionsWe provide an effective strategy to simultaneously improve both thermostability and catalytic efficiency of glucoamylase. The excellent thermostability and high catalytic efficiency of TlGa15B-GA2 make it a good candidate for industrial saccharification applications.
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