Characterization of a novel carboxylesterase with catalytic activity toward di(2-ethylhexyl) phthalate from a soil metagenomic library

2021 ◽  
Vol 785 ◽  
pp. 147260
Author(s):  
Zhenzhen Yan ◽  
Liping Ding ◽  
Dandan Zou ◽  
Jiarong Qiu ◽  
Yuting Shao ◽  
...  
Author(s):  
Zhenzhen Yan ◽  
Liping Ding ◽  
Dandan Zou ◽  
Luyao Wang ◽  
Yuzhi Tan ◽  
...  

Polymers ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1160
Author(s):  
Abir S. Abdel-Naby ◽  
Sara Nabil ◽  
Sarah Aldulaijan ◽  
Ibtisam M. Ababutain ◽  
Azzah I. Alghamdi ◽  
...  

Chitosan-aluminum oxide nanocomposite was synthesized, characterized, and used as a green heterogeneous catalyst to synthesize novel imidazopyrazolylthione derivatives. Nanocomposite polymeric material was characterized by EDS-SEM and XRD. The powerful catalytic activity, and its base character of the nanocomposite, was used to synthesize imidazopyrazolylthione (1) in a good yield compared to traditional cyclocondensation synthesis. Using the nanocomposite catalyst, substitution of the thiol group (1) afforded the corresponding thiourea (2) and the corresponding ester (3). The efficiency of the nanocomposite over the traditional base organic catalyst, Et3N and NaOH, makes it an effective, economic, and reproducible nontoxic catalyst. Moreover, the heterogeneous nanocomposite polymeric film was easily isolated from the reaction medium, and recycled up to four times, without a significant loss of its catalytic activity. The newly synthesized derivatives were screened as antibacterial agents and showed high potency. Molecular docking was also performed for a more in-depth investigation. The results of the docking studies have demonstrated that the docked compounds have strong interaction energies with both Gram-positive and Gram-negative bacteria.


2021 ◽  
Vol 22 (2) ◽  
pp. 734
Author(s):  
Paul K. Varghese ◽  
Mones Abu-Asab ◽  
Emilios K. Dimitriadis ◽  
Monika B. Dolinska ◽  
George P. Morcos ◽  
...  

Human Tyrosinase (Tyr) is the rate-limiting enzyme of the melanogenesis pathway. Tyr catalyzes the oxidation of the substrate L-DOPA into dopachrome and melanin. Currently, the characterization of dopachrome-related products is difficult due to the absence of a simple way to partition dopachrome from protein fraction. Here, we immobilize catalytically pure recombinant human Tyr domain (residues 19–469) containing 6xHis tag to Ni-loaded magnetic beads (MB). Transmission electron microscopy revealed Tyr-MB were within limits of 168.2 ± 24.4 nm while the dark-brown melanin images showed single and polymerized melanin with a diameter of 121.4 ± 18.1 nm. Using Hill kinetics, we show that Tyr-MB has a catalytic activity similar to that of intact Tyr. The diphenol oxidase reactions of L-DOPA show an increase of dopachrome formation with the number of MB and with temperature. At 50 °C, Tyr-MB shows some residual catalytic activity suggesting that the immobilized Tyr has increased protein stability. In contrast, under 37 °C, the dopachrome product, which is isolated from Tyr-MB particles, shows that dopachrome has an orange-brown color that is different from the color of the mixture of L-DOPA, Tyr, and dopachrome. In the future, Tyr-MB could be used for large-scale productions of dopachrome and melanin-related products and finding a treatment for oculocutaneous albinism-inherited diseases.


1996 ◽  
Vol 38 (1-2) ◽  
pp. 33-37 ◽  
Author(s):  
Xiu S. Zhao ◽  
Gao Q. Lu ◽  
Graeme J. Millar ◽  
Xin S. Li

2015 ◽  
Vol 335 ◽  
pp. 23-28 ◽  
Author(s):  
Wei-hong Li ◽  
Xiu-ping Yue ◽  
Chang-sheng Guo ◽  
Jia-pei Lv ◽  
Si-si Liu ◽  
...  

2014 ◽  
Vol 80 (16) ◽  
pp. 4958-4967 ◽  
Author(s):  
Marjolaine Martin ◽  
Sophie Biver ◽  
Sébastien Steels ◽  
Tristan Barbeyron ◽  
Murielle Jam ◽  
...  

ABSTRACTA metagenomic library was constructed from microorganisms associated with the brown algaAscophyllum nodosum. Functional screening of this library revealed 13 novel putative esterase loci and two glycoside hydrolase loci. Sequence and gene cluster analysis showed the wide diversity of the identified enzymes and gave an idea of the microbial populations present during the sample collection period. Lastly, an endo-β-1,4-glucanase having less than 50% identity to sequences of known cellulases was purified and partially characterized, showing activity at low temperature and after prolonged incubation in concentrated salt solutions.


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