Publications by authors named "Jinxue Ma"
Article Synopsis
- Carboxylesterase is an important industrial enzyme used in sectors like fine chemistry and bioremediation, but its limited thermostability poses challenges for industrial use.
- Researchers discovered a novel carboxylesterase (EstF) from Streptomyces lividans TK24 that shows optimal activity at 55 °C and high stability, with a half-life of 387.23 hours at that temperature.
- By using site-directed mutation to introduce a single glycine, the mutant EstF showed a significant increase in half-life at 100 °C without losing catalytic efficiency, suggesting new methods for improving enzyme stability.
Nicotinamide phosphoribosyltransferase (NAMPT) plays an important role in the biosynthesis of nicotinamide adenine dinucleotide (NAD) via the nicotinamide (NAM) salvage pathway. While the structural biochemistry of eukaryote NAMPT has been well studied, the catalysis mechanism of prokaryote NAMPT at the molecular level remains largely unclear. Here, we demonstrated the NAMPT-mediated salvage pathway is functional in the Gram-negative phytopathogenic bacterium Xanthomonas campestris pv.
View Article and Find Full Text PDFCarboxylesterases have widely been used in a series of industrial applications, especially, the detoxification of pesticide residues. In the present study, EstC, a novel carboxylesterase from Streptomyces lividans TK24, was successfully heterogeneously expressed, purified and characterized. Phylogenetic analysis showed that EstC can be assigned as the first member of a novel family XIX.
View Article and Find Full Text PDFAim: To evaluate the optical performance of toric intraocular lenses (IOLs) after decentration and with different pupil diameters, but with the IOL astigmatic axis aligned.
Methods: Optical performances of toric T5 and SN60AT spherical IOLs after decentration were tested on a theoretical pseudophakic model eye based on the Hwey-Lan Liou schematic eye using the Zemax ray-tracing program. Changes in optical performance were analyzed in model eyes with 3-mm, 4-mm, and 5-mm pupil diameters and decentered from 0.