Development of a catalytically stable and efficient lipase through an increase in hydrophobicity of the oxyanion residue-Reference-Cited by-同舟云学术

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Development of a catalytically stable and efficient lipase through an increase in hydrophobicity of the oxyanion residue

Published:2015-12 Issue: Volume:122 Page:282-288
ISSN:1381-1177
Container-title:Journal of Molecular Catalysis B: Enzymatic
language:en
Short-container-title:Journal of Molecular Catalysis B: Enzymatic

Author:

Abdul Wahab Roswanira,Basri Mahiran,Raja Abdul Rahman Raja Noor Zaliha,Salleh Abu Bakar,Abdul Rahman Mohd Basyaruddin,Leow Thean Chor

Publisher

Elsevier BV

Subject

Process Chemistry and Technology,Biochemistry,Bioengineering,Catalysis

Reference38 articles.

1. The effect of cavity-filling mutations on the thermostability of Bacillus stearothermophilus neutral protease

2. Forces contributing to the conformational stability of proteins

3. Stability of folded conformations

4. Internal packing of helical membrane proteins

5. Stabilization of hen egg white lysozyme by a cavity-filling mutation

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1. Development of a new Geobacillus lipase variant GDlip43 via directed evolution leading to identification of new activity-regulating amino acids;International Journal of Biological Macromolecules;2020-05

2. Lipase-Catalyzed Synthesis of Sn-2 Palmitate: A Review;Engineering;2020-04

3. Molecular docking and molecular dynamics simulations of a mutant Acinetobacter haemolyticus alkaline-stable lipase against tributyrin;Journal of Biomolecular Structure and Dynamics;2020-03-23

4. 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 and Biotechnology;2020-02-27

5. Improving the Catalytic Activity and Thermostability of MAS1 Lipase by Alanine Substitution;Molecular Biotechnology;2018-02-15

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