Page last updated: 2024-08-25

mandelamide and mandelic acid

mandelamide has been researched along with mandelic acid in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Kenyon, GL; McLeish, MJ; Wang, PF; Yep, A	1
Kiziak, C; Stolz, A	1

Other Studies

2 other study(ies) available for mandelamide and mandelic acid

Article	Year
Using directed evolution to probe the substrate specificity of mandelamide hydrolase. Protein engineering, design & selection : PEDS, 2009, Volume: 22, Issue:2 Topics: Amides; Amidohydrolases; Ammonia; Bacterial Proteins; Catalytic Domain; Directed Molecular Evolution; Escherichia coli; Gene Library; Mandelic Acids; Mutagenesis, Site-Directed; Mutation; Protein Engineering; Pseudomonas putida; Substrate Specificity	2009
Identification of amino acid residues responsible for the enantioselectivity and amide formation capacity of the Arylacetonitrilase from Pseudomonas fluorescens EBC191. Applied and environmental microbiology, 2009, Volume: 75, Issue:17 Topics: Acetonitriles; Alcaligenes faecalis; Amino Acid Substitution; Aminohydrolases; Catalytic Domain; Mandelic Acids; Mutagenesis, Site-Directed; Pseudomonas fluorescens; Recombinant Fusion Proteins; Stereoisomerism; Substrate Specificity	2009

Article

Year

Using directed evolution to probe the substrate specificity of mandelamide hydrolase.

Protein engineering, design & selection : PEDS, 2009, Volume: 22, Issue:2

Topics: Amides; Amidohydrolases; Ammonia; Bacterial Proteins; Catalytic Domain; Directed Molecular Evolution; Escherichia coli; Gene Library; Mandelic Acids; Mutagenesis, Site-Directed; Mutation; Protein Engineering; Pseudomonas putida; Substrate Specificity

2009

Identification of amino acid residues responsible for the enantioselectivity and amide formation capacity of the Arylacetonitrilase from Pseudomonas fluorescens EBC191.

Applied and environmental microbiology, 2009, Volume: 75, Issue:17

Topics: Acetonitriles; Alcaligenes faecalis; Amino Acid Substitution; Aminohydrolases; Catalytic Domain; Mandelic Acids; Mutagenesis, Site-Directed; Pseudomonas fluorescens; Recombinant Fusion Proteins; Stereoisomerism; Substrate Specificity

2009