ArticleScientific reports2016
Truncation of the unique N-terminal domain improved the thermos-stability and specific activity of alkaline α-amylase Amy703.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Biochemical and structural characterization of AmyY fromApplied and environmental microbiology · 2026Article
- N-terminal truncated phospholipase A1 accessory protein PlaS from Serratia marcescens alleviates inhibitory on host cell growth and enhances PlaA1 enzymatic activity.Bioresources and bioprocessing · 2024Article
- Analyzing Current Trends and Possible Strategies to Improve Sucrose Isomerases' Thermostability.International journal of molecular sciences · 2023Review
- AmyJ33, a truncated amylase with improved catalytic properties.Biotechnology letters · 2022Article
- Simultaneously improving the specific activity and thermostability of α-amylase BLA by rational design.Bioprocess and biosystems engineering · 2022Article
- Engineering mesophilic GH11 xylanase fromFrontiers in bioengineering and biotechnology · 2022Article
- Highly Efficient Computationally Derived Novel Metagenome α-Amylase With Robust Stability Under Extreme Denaturing Conditions.Frontiers in microbiology · 2021Article
- Single Residue Substitution atMolecules (Basel, Switzerland) · 2020Article
- A hybrid of two major Blomia tropicalis allergens as an allergy vaccine candidate.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2020Article
- Tunnel engineering to accelerate product release for better biomass-degrading abilities in lignocellulolytic enzymes.Biotechnology for biofuels · 2019Article
- The response to selection in Glycoside Hydrolase Family 13 structures: A comparative quantitative genetics approach.PloS one · 2018Article
- Two-Dimensional Gel Electrophoresis-Based Proteomic Analysis Reveals N-terminal Truncation of the Hsc70 Protein in Cotton Fibers In Vivo.Scientific reports · 2016Article
- A general and efficient strategy for generating the stable enzymes.Scientific reports · 2016Article
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Authors and funding
5 authors.
Funding
Abstract
High pH condition is of special interest for the potential applications of alkaline α-amylase in textile and detergent industries. Thus, there is a continuous demand to improve the amylase's properties to meet the requirements set by specific applications. Here we reported the systematic study of modular domain engineering to improve the specific activity and stability of the alkaline α-amylase from Bacillus pseudofirmus 703. The specific activity of the N-terminal domain truncated mutant (N-Amy) increased by ~35-fold with a significantly improved thermo-stability. Kinetic analysis demonstrated that the Kcat and Kcat/Kmof N-Amy were enhanced by 1300-fold and 425.7-fold, respectively, representing the largest catalytic activity improvement of the engineered α-amylases through the methods of domain deletion, fusion or swapping. In addition, different from the wild-type Amy703, no exogenous Ca(2+) were required for N-Amy to maintain its full catalytic activity, implying its superior potential for many industrial processes. Circular dichroism analysis and structure modeling revealed that the increased compactness and α-helical content were the main contributors for the improved thermo-stability of N-Amy, while the improved catalytic efficiency was mainly attributed by the increased conformational flexibility around the active center.
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