A5071616619- Enzyme Catalysis and Immobilization
- GABA and Rice Research
- Probiotics and Fermented Foods
- Microbial Metabolic Engineering and Bioproduction
- Biochemical effects in animals
- Carbohydrate Chemistry and Synthesis
- Chemical Synthesis and Analysis
- Amino Acid Enzymes and Metabolism
- Protein Hydrolysis and Bioactive Peptides
- Biochemical and Molecular Research
- Glycosylation and Glycoproteins Research
- Ionic liquids properties and applications
- Tryptophan and brain disorders
- RNA and protein synthesis mechanisms
- Mitochondrial Function and Pathology
Jiangnan University
2025
Zhejiang University of Science and Technology
2019-2023
Transaminases that promote the amination of ketones into amines are an emerging class biocatalysts for preparing a series drugs and their intermediates. One main limitations ( R )-selective amine transaminase from Aspergillus terreus At -ATA) is its weak thermostability, with half-life t 1/2 ) only 6.9 min at 40°C. To improve four important residue sites (E133, D224, E253, E262) located on surface -ATA were identified using enzyme thermal stability system (ETSS). Subsequently, 13 mutants...
Amine transaminases (ATAs) catalyze the asymmetric amination of prochiral ketones or aldehydes to their corresponding chiral amines. However, trade-off between activity and stability in enzyme engineering represents a major obstacle practical application ATAs. Overcoming this is important for developing robustly engineered enzymes universal approach Herein, we modified binding pocket ω-ATA from Aspergillus terreus (AtATA) identify key amino acid residues controlling AtATA toward...
ω-transaminase (ω-TA) is a natural biocatalyst that has good application potential in the synthesis of chiral amines. However, poor stability and low activity ω-TA process catalyzing unnatural substrates greatly hampers its application. To overcome these shortcomings, thermostability (R)-ω-TA (AtTA) from Aspergillus terreus was engineered by combining molecular dynamics simulation assisted computer-aided design with random combinatorial mutation. An optimal mutant AtTA-E104D/A246V/R266Q (M3)...
Abstract Objectives γ-Aminobutyric acid (GABA) is a non-protein amino acid, considered potent bioactive compound. This study focused on biosynthesis of food-grade GABA by immobilized glutamate decarboxylase (GAD) from Lactobacillus plantarum in the rice vinegar and monosodium (MSG) reaction system. Results The gene encoding GadB L. has been heterologously expressed Lactococcus lactis biochemically characterized. Recombinant existed as homodimer, displayed maximal activity at 40℃ pH 5.0. K m...