scholarly journals Improving the Stability and Catalyst Lifetime of the Halogenase RebH By Directed Evolution

ChemBioChem ◽  
2014 ◽  
Vol 15 (9) ◽  
pp. 1286-1289 ◽  
Author(s):  
Catherine B. Poor ◽  
Mary C. Andorfer ◽  
Jared C. Lewis
Keyword(s):  
Directed Evolution ◽  
The Stability ◽  
Catalyst Lifetime

Directed Evolution of a Formate Dehydrogenase for Increased Tolerance to Ionic Liquids Reveals a New Site for Increasing the Stability

ChemBioChem ◽  
2014 ◽  
Vol 15 (18) ◽  
pp. 2710-2718 ◽  
Author(s):  
Julie L. L. Carter ◽  
Mourad Bekhouche ◽  
Alexandre Noiriel ◽  
Loïc J. Blum ◽  
Bastien Doumèche
Keyword(s):  
Ionic Liquids ◽  
Directed Evolution ◽  
Formate Dehydrogenase ◽  
The Stability

Improvement of the stability and activity of the BPO-A1 haloperoxidase from Streptomyces aureofaciens by directed evolution

2014 ◽  
Vol 192 ◽  
pp. 248-254 ◽  
Author(s):  
Ryosuke Yamada ◽  
Tatsutoshi Higo ◽  
Chisa Yoshikawa ◽  
Hideyasu China ◽  
Hiroyasu Ogino
Keyword(s):  
Directed Evolution ◽  
Streptomyces Aureofaciens ◽  
The Stability

scholarly journals Directed Evolution and Immobilization of a Novel Lipase LIP 906

2020 ◽  
Author(s):  
Shuang Dai ◽  
He Li
Keyword(s):  
Enzyme Activity ◽  
Directed Evolution ◽  
Early Stage ◽  
Temperature Stability ◽  
Mutant Enzyme ◽  
Random Mutation ◽  
Optimum Reaction ◽  
Pcr Technology ◽  
Solid Foundation ◽  
The Stability

Abstract Background: The object of this experimental study is a new lipase screened from metagenomic libraries in the early stage of the laboratory and named it LIP 906. In order to improve the stability of the enzyme and develop and apply it as soon as possible, experiments use directed evolution and immobilization.Results: A random mutation library was constructed by error-prone PCR technology, and finally a mutant lipase LIP 5-D with improved enzyme activity was screened out and then immobilized. Compared with the wild-type lipase LIP 906, the enzyme activity of the mutant enzyme LIP 5-D increased 4 times; the optimum reaction temperature was increased by 4 °C by mutation and 3 ℃ by immobilization; and the optimum reaction pH is changed from 7.8 to 7.5; temperature stability and pH stability has been improved. The mutant enzyme LIP 5-D can maintain a relative enzyme activity of about 70% at a temperature below 65 °C for 2 hours, and can also maintain a relative enzyme activity of about 60% at different pH 3 -10.Conclusions: Error-prone PCR and immobilization improved the catalytic activity and stability of the enzyme, and promoted its development and application in many industries. The research on the properties and modification of the new lipase LIP906 provides a solid foundation for my next innovative research in application and environmental protection.

Synthesis of hierarchical ZSM-5 nano-aggregated microspheres for the application in enhancing the stability of n-hexane aromatization

2021 ◽  
Author(s):  
Xiongfu ZHANG ◽  
Jinshan Wang ◽  
Cun Liu ◽  
Peng Zhu ◽  
Haiou Liu ◽  
...  
Keyword(s):  
Hierarchical Structure ◽  
Light Alkanes ◽  
Important Approach ◽  
The Stability ◽  
Catalyst Lifetime

Incorporating mesopores into ZSM-5 zeolite for forming hierarchical structure has been regarded as an important approach to enhance the diffusivity and catalyst lifetime for light alkanes aromatization. Herein, hierarchical ZSM-5...

scholarly journals Directed evolution and immobilization of new lipase Lip 906

2021 ◽  
Vol 233 ◽  
pp. 02030
Author(s):  
Shuang Dai ◽  
Shan Liu ◽  
Yun Jeonyun ◽  
Xiong Xiao ◽  
Zujun Deng ◽  
...  
Keyword(s):  
Directed Evolution ◽  
Metagenomic Library ◽  
Temperature Stability ◽  
Relative Activity ◽  
Mutant Enzyme ◽  
Wild Type ◽  
Random Mutation ◽  
Optimal Reaction Temperature ◽  
The Stability ◽  
Optimal Reaction

In this experimental study, a new lipase named Lip 906 was screened out from a metagenomic library in the laboratory. To improve the stability of the enzyme and develop and apply it as soon as possible, we adopted directed evolution and immobilization methods. A random mutation library was constructed by error-prone PCR and finally, a mutant lipase Lip 5-D with increased enzyme activity was screened out and immobilized. The activity of the mutant enzyme Lip 5-D was improved by 4 times compared with the wild-type lipase Lip 906. The optimal reaction temperature rose by 4 °C, and by 3 °C after immobilization. The optimal reaction pH increased from 7.8 to 7.5. Both temperature stability and pH stability were improved. The mutant enzyme Lip 5-D can maintain about 70% of the relative activity after incubation at 65 °C for 2 h, and it can keep 60% at pH 3-10. Error-prone PCR and immobilization improve the catalytic activity and stability of the enzyme, and promote its development and application in many industries.

Increased Rigidity of Domain Structures Enhances the Stability of a Mutant Enzyme Created by Directed Evolution†

Biochemistry ◽  
2003 ◽  
Vol 42 (49) ◽  
pp. 14469-14475 ◽  
Author(s):  
Jun Hoseki ◽  
Akihiro Okamoto ◽  
Naoki Takada ◽  
Atsushi Suenaga ◽  
Noriyuki Futatsugi ◽  
...  
Keyword(s):  
Directed Evolution ◽  
Mutant Enzyme ◽  
Domain Structures ◽  
The Stability

Open discussion

1982 ◽  
Vol 99 ◽  
pp. 605-613
Author(s):  
P. S. Conti
Keyword(s):  
Buenos Aires ◽  
Large Mass ◽  
List Type ◽  
Common Phenomenon ◽  
Open Discussion ◽  
The Stability ◽  
Ring Nebulae

Conti: One of the main conclusions of the Wolf-Rayet symposium in Buenos Aires was that Wolf-Rayet stars are evolutionary products of massive objects. Some questions:–Do hot helium-rich stars, that are not Wolf-Rayet stars, exist?–What about the stability of helium rich stars of large mass? We know a helium rich star of ∼40 MO. Has the stability something to do with the wind?–Ring nebulae and bubbles : this seems to be a much more common phenomenon than we thought of some years age.–What is the origin of the subtypes? This is important to find a possible matching of scenarios to subtypes.

Symmetric Multistep Methods Revisited: II. Numerical Experiments

1999 ◽  
Vol 173 ◽  
pp. 309-314 ◽  
Author(s):  
T. Fukushima
Keyword(s):  
Multistep Methods ◽  
Computational Time ◽  
Integration Time ◽  
Implicit Methods ◽  
Symmetric Methods ◽  
Celestial Bodies ◽  
The Stability ◽  
Predictor Corrector ◽  
Symmetric Multistep Methods ◽  
Integration Errors

AbstractBy using the stability condition and general formulas developed by Fukushima (1998 = Paper I) we discovered that, just as in the case of the explicit symmetric multistep methods (Quinlan and Tremaine, 1990), when integrating orbital motions of celestial bodies, the implicit symmetric multistep methods used in the predictor-corrector manner lead to integration errors in position which grow linearly with the integration time if the stepsizes adopted are sufficiently small and if the number of corrections is sufficiently large, say two or three. We confirmed also that the symmetric methods (explicit or implicit) would produce the stepsize-dependent instabilities/resonances, which was discovered by A. Toomre in 1991 and confirmed by G.D. Quinlan for some high order explicit methods. Although the implicit methods require twice or more computational time for the same stepsize than the explicit symmetric ones do, they seem to be preferable since they reduce these undesirable features significantly.

Uniformity of Magnification from Different Electron Microscopes

1967 ◽  
Vol 25 ◽  
pp. 32-33
Author(s):  
Godfrey C. Hoskins ◽  
V. Williams ◽  
V. Allison
Keyword(s):  
Diffraction Grating ◽  
The Other ◽  
Carbon Replica ◽  
Electron Microscopes ◽  
The Stability

The method demonstrated is an adaptation of a proven procedure for accurately determining the magnification of light photomicrographs. Because of the stability of modern electrical lenses, the method is shown to be directly applicable for providing precise reproducibility of magnification in various models of electron microscopes.A readily recognizable area of a carbon replica of a crossed-line diffraction grating is used as a standard. The same area of the standard was photographed in Phillips EM 200, Hitachi HU-11B2, and RCA EMU 3F electron microscopes at taps representative of the range of magnification of each. Negatives from one microscope were selected as guides and printed at convenient magnifications; then negatives from each of the other microscopes were projected to register with these prints. By deferring measurement to the print rather than comparing negatives, correspondence of magnification of the specimen in the three microscopes could be brought to within 2%.

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