ArticlePloS one2016
Improving the Thermostability of Acidic Pullulanase from Bacillus naganoensis by Rational Design.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 27 citations in OpenAlex.
- Pullulanase: unleashing the power of enzyme with a promising future in the food industry.Frontiers in bioengineering and biotechnology · 2023Review
- Pullulanase with high temperature and low pH optima improved starch saccharification efficiency.Scientific reports · 2022Article
- Biotechnology and bioengineering of pullulanase: state of the art and perspectives.World journal of microbiology & biotechnology · 2021Review
- Genetically Modified Micro-Organisms for Industrial Food Enzyme Production: An Overview.Foods (Basel, Switzerland) · 2020Review
- Evolutionary coupling saturation mutagenesis: Coevolution-guided identification of distant sites influencing Bacillus naganoensis pullulanase activity.FEBS letters · 2020Article
- Understanding Thermostability Factors of Barley Limit Dextrinase by Molecular Dynamics Simulations.Frontiers in molecular biosciences · 2020Article
- Disulfide Bond Engineering of an Endoglucanase fromInternational journal of molecular sciences · 2019Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pullulanase (EC 3.2.1.41) plays an important role in the specific hydrolysis of branch points in amylopectin. Enhancing its thermostability is required for its industrial application. In this study, rational protein design was used to improve the thermostability of PulB from Bacillus naganoensis (AB231790.1), which has strong enzymatic properties. Three positive single-site mutants (PulB-D328H, PulB-N387D, and PulB-A414P) were selected from six mutants. After incubation at 65°C for 5 min, the residual activities of PulB-D328H, PulB-N387D, and PulB-A414P were 4.5-, 1.7-, and 1.47-fold higher than PulB-WT, and their Tm values (the temperature at which half protein molecule denature) were 1.8°C, 0.4°C, and 0.9°C higher than PulB-WT, respectively. Then the final combined mutant PulB-328/387/414 was constructed. The t1/2 of it was 12.9-fold longer than that of PulB-WT at 65°C and the total increase in Tm of it (5.0°C) was almost 60% greater than the sum of individual increases (3.1°C). In addition, kinetic studies revealed that the kcat and the kcat/Km of PulB-328/387/414 increased by 38.8% and 12.9%. The remarkable improvement in thermostability and the high catalytic efficiency of PulB-328/387/414 make it suitable for industrial applications.
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