ArticleInternational journal of molecular sciences2012
Improvement of thermal stability via outer-loop ion pair interaction of mutated T1 lipase from Geobacillus zalihae strain T1.
Article in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Thermostable Bacterial Esterases From Lipase Family 1.5 Degrade Compostable Polyesters PBAT and PBSA.MicrobiologyOpen · 2025Article
- A Lipase Gene ofInternational journal of molecular sciences · 2024Article
- Identification, Characterization, and Computer-Aided Rational Design of a Novel Thermophilic Esterase from Geobacillus subterraneus, and Application in the Synthesis of Cinnamyl Acetate.Applied biochemistry and biotechnology · 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
- An Appraisal on Prominent Industrial and Biotechnological Applications of Bacterial Lipases.Molecular biotechnology · 2023Review
- Cold Active Lipases: Biocatalytic Tools for Greener Technology.Applied biochemistry and biotechnology · 2021Review
- Decoding the intricate network of molecular interactions of a hyperstable engineered biocatalyst.Chemical science · 2020Article
- Single Residue Substitution atMolecules (Basel, Switzerland) · 2020Article
- New engineered Geobacillus lipase GD-95RM for industry focusing on the cleaner production of fatty esters and household washing product formulations.World journal of microbiology & biotechnology · 2020Article
- Enhancing the Thermostability of Rhizomucor miehei Lipase with a Limited Screening Library by Rational-Design Point Mutations and Disulfide Bonds.Applied and environmental microbiology · 2018Article
- Realm of Thermoalkaline Lipases in Bioprocess Commodities.Journal of lipids · 2018Review
- Ability of T1 Lipase to Degrade Amorphous P(3HB): Structural and Functional Study.Molecular biotechnology · 2017Article
- From structure to catalysis: recent developments in the biotechnological applications of lipases.BioMed research international · 2014Review
- The conserved lid tryptophan, W211, potentiates thermostability and thermoactivity in bacterial thermoalkalophilic lipases.PloS one · 2013Article
- Lipase improvement: goals and strategies.Computational and structural biotechnology journal · 2012Review
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6 authors.
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Abstract
Mutant D311E and K344R were constructed using site-directed mutagenesis to introduce an additional ion pair at the inter-loop and the intra-loop, respectively, to determine the effect of ion pairs on the stability of T1 lipase isolated from Geobacillus zalihae. A series of purification steps was applied, and the pure lipases of T1, D311E and K344R were obtained. The wild-type and mutant lipases were analyzed using circular dichroism. The T(m) for T1 lipase, D311E lipase and K344R lipase were approximately 68.52 °C, 70.59 °C and 68.54 °C, respectively. Mutation at D311 increases the stability of T1 lipase and exhibited higher T(m) as compared to the wild-type and K344R. Based on the above, D311E lipase was chosen for further study. D311E lipase was successfully crystallized using the sitting drop vapor diffusion method. The crystal was diffracted at 2.1 Å using an in-house X-ray beam and belonged to the monoclinic space group C2 with the unit cell parameters a = 117.32 Å, b = 81.16 Å and c = 100.14 Å. Structural analysis showed the existence of an additional ion pair around E311 in the structure of D311E. The additional ion pair in D311E may regulate the stability of this mutant lipase at high temperatures as predicted in silico and spectroscopically.
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