scholarly journals Cover Feature: Distance between Metal Centres Affects Catalytic Efficiency of Dinuclear CoIII Complexes in the Hydrolysis of a Phosphate Diester (Eur. J. Org. Chem. 39/2018)

2018 ◽  
Vol 2018 (39) ◽  
pp. 5335-5335
Author(s):  
Eva Szusanna Bencze ◽  
Cristiano Zonta ◽  
Fabrizio Mancin ◽  
Leonard J. Prins ◽  
Paolo Scrimin
Keyword(s):  
Catalytic Efficiency ◽  
Phosphate Diester ◽  
Hydrolysis Of

The Study of the Hydrolysis of the Phosphate Diester Catalyzed by an Anion Metallomicelle of Ce3+-Diethylenetriamine

2012 ◽  
Vol 554-556 ◽  
pp. 353-356
Author(s):  
Shu Lan Cai ◽  
Fa Mei Feng ◽  
Tao Wang ◽  
Xiu Lan Zhang
Keyword(s):  
Critical Micelle Concentration ◽  
High Activity ◽  
Catalytic Efficiency ◽  
Active Species ◽  
Phosphate Ester ◽  
Catalytic Hydrolysis ◽  
Phosphate Diester ◽  
Nitrophenyl Phosphate ◽  
Hydrolysis Of ◽  
Lauroyl Sarcosinate

The catalytic hydrolysis of Bis(p-nitrophenyl) phosphate ester (BNPP) in the metallomicelle made up of Ce3+-diethylenetriamine and LSS (N-lauroyl sarcosinate) was investigated by UV/VIS method. The effect of the catalytic efficiency and stability of the system was studied under the different conditions. The results indicated that the catalytic system exhibited high activity, stability and reproducibility in the BNPP catalytic hydrolysis under proper proportion of Ce3+ion and diethylenetriamine, pH and temperature when the concentration of LSS is higher than its CMC (critical micelle concentration). The results also showed that the active species is the complex made up of Ce3+ion and diethylenetriamine.

Distance between Metal Centres Affects Catalytic Efficiency of Dinuclear CoIII Complexes in the Hydrolysis of a Phosphate Diester

2018 ◽  
Vol 2018 (39) ◽  
pp. 5375-5381 ◽  
Author(s):  
Eva Szusanna Bencze ◽  
Cristiano Zonta ◽  
Fabrizio Mancin ◽  
Leonard J. Prins ◽  
Paolo Scrimin
Keyword(s):  
Catalytic Efficiency ◽  
Phosphate Diester ◽  
Hydrolysis Of

Catalytic Hydrolysis of Phosphate Diester with Metal Complexes of Macrocyclic Tetraamine in Comicellar Solution

2010 ◽  
Vol 19 (2) ◽  
pp. 158-163 ◽  
Author(s):  
Qing-Xiang Xiang ◽  
Xiao-Qi Yu ◽  
Jing-Song You ◽  
Qian-Shun Yan ◽  
Rn-Gang Xie
Keyword(s):  
Metal Complexes ◽  
Catalytic Hydrolysis ◽  
Phosphate Diester ◽  
Hydrolysis Of

scholarly journals Application of β-glucosidase Immobilized on Chitosan microspheres in Degradation of Polydatin in Polygonum cuspidatum

2021 ◽  
Vol 233 ◽  
pp. 02034
Author(s):  
Wei Zong ◽  
Shan Liu ◽  
Jeonyun Yun ◽  
Xiong Xiao ◽  
Zujun Deng ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Cost Reduction ◽  
Degradation Rate ◽  
Temperature Stability ◽  
Catalytic Efficiency ◽  
Efficient Production ◽  
Polygonum Cuspidatum ◽  
Optimum Temperature ◽  
Preparation Conditions ◽  
Hydrolysis Of

Resveratrol in Polygonum cuspidatum is a β-glycoside, which can be hydrolyzed to resveratrol by β-glucosidase. it is an efficient production process to degrade polydatin from Polygonum cuspidatum extract by immobilized β-glucosidase. It is of great significance to explore suitable immobilization conditions to improve the catalytic efficiency and reusability of β-glucosidase for polydatin degradation and cost reduction. In this paper, the recombinant Escherichia coli bgl2238, which was screened and constructed from corn soil of Heilongjiang Province in the early laboratory, was immobilized by chitosan adsorption and glutaraldehyde crosslinking. The preparation conditions and immobilization process of bgl2238 were determined by single factor method: the optimal crosslinking time was 1 h, the optimal crosslinking temperature was 20 °C, the recovery rate of enzyme activity of bgl2238 was 87 %, and the enzyme activity was 859.65 mU/g. The optimum temperature of the immobilized bgl2238 is 50 °C, which is 6 °C higher than that of the free bgl2238, and the temperature stability and pH stability are improved. After six consecutive hydrolysis of Polygonum cuspidatum, the degradation rate of polydatin is still over 70 %, which proves that the immobilized bgl2238 has good reusability. This will be helpful to evaluate the application prospect of β - glucosidase immobilized in this system and determine the best conditions for its production.

scholarly journals Mutational Effects on Carbapenem Hydrolysis of YEM-1, a New Subclass B2 Metallo-β-Lactamase from Yersinia mollaretii

2020 ◽  
Vol 64 (9) ◽  
Author(s):  
Paola Sandra Mercuri ◽  
Roberto Esposito ◽  
Sylvie Blétard ◽  
Stefano Di Costanzo ◽  
Mariagrazia Perilli ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Catalytic Efficiency ◽  
The Other ◽  
Kinetic Characterization ◽  
Activity Profile ◽  
Gene Encoding ◽  
Content Type ◽  
Hydrolysis Of

ABSTRACT Analysis of the genome sequence of Yersinia mollaretii ATCC 43969 identified the blaYEM gene, encoding YEM-1, a putative subclass B2 metallo-β-lactamase. The objectives of our work were to produce and purify YEM-1 and to complete its kinetic characterization. YEM-1 displayed the narrowest substrate range among known subclass B2 metallo-β-lactamases, since it can hydrolyze imipenem, but not other carbapenems, such as biapenem, meropenem, doripenem, and ertapenem, with high catalytic efficiency. A possible explanation of this activity profile is the presence of tyrosine at residue 67 (loop L1), threonine at residue 156 (loop L2), and serine at residue 236 (loop L3). We showed that replacement of Y67 broadened the activity profile of the enzyme for all carbapenems but still resulted in poor activity toward the other β-lactam classes.

Sign in / Sign up

Export Citation Format

Share Document