Thermostabilization of porcine kidneyD-amino acid oxidase by a single amino acid substitution
Author:
Publisher
Wiley
Subject
Applied Microbiology and Biotechnology,Bioengineering,Biotechnology
Reference22 articles.
1. Improvement in Thermal Stability and Substrate Binding of Pig Kidney D-Amino Acid Oxidase by Chemical Modification
2. Use of Physicochemical Tools to Determine the Choice of Optimal Enzyme: Stabilization of -Amino Acid Oxidase
3. Mutagenic PCR.
4. Improved purification, amino acid analysis and molecular weight of homogeneous d-amino acid oxidase from pig kidney
5. Chemistry, Nutrition, and Microbiology of d-Amino Acids
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1. Kinetics of Thermoinactivation of D-Amino Acid Oxidase OPADAAO1 from the Ogataea parapolymorpha DL-1 Yeast;Moscow University Chemistry Bulletin;2023-04
2. The Stability of Dimeric D-amino Acid Oxidase from Porcine Kidney Strongly Depends on the Buffer Nature and Concentration;Catalysts;2022-09-06
3. Enzyme assay for d -amino acid oxidase using optically gated capillary electrophoresis-laser induced fluorescence detection;Journal of Chromatography A;2018-05
4. Enhancement of the solubility and stability of d-amino acid oxidase by fusion to an elastin like polypeptide;Journal of Biotechnology;2015-10
5. A Highly Stable d-Amino Acid Oxidase of the Thermophilic Bacterium Rubrobacter xylanophilus;Applied and Environmental Microbiology;2014-09-12
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