P
Praveen Kaul
Researcher at Department of Biotechnology
Publications - 12
Citations - 554
Praveen Kaul is an academic researcher from Department of Biotechnology. The author has contributed to research in topics: Nitrilase & Mandelonitrile. The author has an hindex of 10, co-authored 12 publications receiving 528 citations.
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Journal ArticleDOI
Screening for enantioselective nitrilases : Kinetic resolution of racemic mandelonitrile to (R)-(-)-mandelic acid by new bacterial isolates
TL;DR: P. putida was found to be the most suitable biocatalyst for further studies as it showed higher reaction rate, lower K m, better growth rate, good yield and ee values and higher stability compared to the other two microorganisms.
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Purification and characterization of an enantioselective arylacetonitrilase from Pseudomonas putida
TL;DR: Higher stability of the enzyme at slightly alkaline pH and ambient temperature provides an excellent opportunity to establish a dynamic kinetic resolution process for the production of (R)-(−)-mandelic acid from readily available mandelonitrile.
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A High-Throughput Amenable Colorimetric Assay for Enantioselective Screening of Nitrilase-Producing Microorganisms Using pH Sensitive Indicators
TL;DR: The method was used to screen a library of nitrilase-producing microorganisms, isolated in the authors' laboratory for their ability to enantioselectively hydrolyze mandelonitrile to mandelic acid, an important chiral building block.
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Stereoselective nitrile hydrolysis by immobilized whole-cell biocatalyst.
TL;DR: The present work attempts to deal with the stability and reusability aspect of nitrilase from Alcaligenes faecalis for the production of (R)-(-)-mandelic acid with 97% enantiomeric excess.
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Enhancing the catalytic potential of nitrilase from Pseudomonas putida for stereoselective nitrile hydrolysis
TL;DR: An inducer feeding approach is suggested to achieve enhanced enzyme production and therefore higher degree of conversion of mandelonitrile, and the addition of the inducer was delayed by 6 h to achieve maximum nitrilase activity.