Improved method for expression and isolation of the Mycoplasma hominis arginine deiminase from the recombinant strain of Escherichia coli

2013 ◽  
Vol 167 (4) ◽  
pp. 420-426 ◽  
Author(s):  
Lyubov R. Fayura ◽  
Yuriy R. Boretsky ◽  
Yuriy V. Pynyaha ◽  
Denys N. Wheatley ◽  
Andriy A. Sibirny
Keyword(s):  
Escherichia Coli ◽  
Recombinant Strain ◽  
Mycoplasma Hominis ◽  
Arginine Deiminase ◽  
Improved Method

Study on Optimization of Fermentation Condition for Nitrilase-Producer Escherichia Coli BL21 (DE3)/pET-Nit

2011 ◽  
Vol 175-176 ◽  
pp. 192-196 ◽  
Author(s):  
Li Li Feng ◽  
Jian Fei Zhang ◽  
Hui Luo ◽  
Zheng Li ◽  
Hong Jie Zhang
Keyword(s):  
Escherichia Coli ◽  
Recombinant Strain ◽  
Culture Medium ◽  
Culture Conditions ◽  
Fermentation Condition ◽  
Hydrogen Phosphate ◽  
Strain Bl21 ◽  
Initial Ph ◽  
Potassium Hydrogen ◽  
Optimization Of Fermentation

The paper concentrated on the optimization of the recombinant strain BL21 (DE3)-PE7-Nit. The component of culture medium and the culture conditions were optimized. The optimized medium was: yeast extract 10 g/l, L-glutamate sodium 8 g/l, MgSO4.7H2O 0.7 g/l, Isopropyl-β-D-thiogalactopyranoside 0.3 mmol/L, potassium hydrogen phosphate 0.5 g / L, phosphate Potassium 0.5 g / L and the culture condition was: initial pH 7.0, inoculum 2%. The result showed that the activity of nitrilase prepared with these conditions increased by 130.37 % through optimization.

scholarly journals An Improved Method of Preparing High Efficiency Transformation Escherichia coli with Both Plasmids and Larger DNA Fragments

2018 ◽  
Vol 58 (4) ◽  
pp. 448-456 ◽  
Author(s):  
Jingjing Liu ◽  
Wenwen Chang ◽  
Lei Pan ◽  
Xiaoyun Liu ◽  
Lufang Su ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Efficiency ◽  
Dna Fragments ◽  
Improved Method

scholarly journals The specificity of a 7 α-hydroxy steroid dehydrogenase from Escherichia coli

1976 ◽  
Vol 157 (1) ◽  
pp. 207-210 ◽  
Author(s):  
E S Haslewood ◽  
G A D Haslewood
Keyword(s):  
Escherichia Coli ◽  
Crude Enzyme ◽  
Hydroxyl Group ◽  
Side Chain ◽  
Improved Method ◽  
Hydroxy Steroid ◽  
Steroid Dehydrogenase

1. Thirty-eight steroids were tested as substrates for a 7 alpha-hydroxy steroid dehydrogenase preparation from a strain of Escherichia coli; an improved method of making the crude enzyme is described. 2. Steroids having a 7 alpha-hydroxyl group in the molecule were substrates except (a) when the 5 beta-cholan-24-oic acid side chain was shortened to less than four carbon atoms and (b) in certain cases when sulphate ester groups were present in the molecule. 3. For testing with the enzyme, a new specimen of 7 alpha-hydroxy-3,12-dioxo-5 beta-cholan-24-oic acid was made, which had properties different from those previously described.

scholarly journals Use of a Recombinant Strain of Mycobacterium avium Expressing β-Galactosidase To Evaluate the Activities of Antimycobacterial Agents inside Macrophages

2001 ◽  
Vol 45 (1) ◽  
pp. 356-358 ◽  
Author(s):  
Giuseppantonio Maisetta ◽  
Giovanna Batoni ◽  
Manuela Pardini ◽  
Antonella Boschi ◽  
Daria Bottai ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Mycobacterium Avium ◽  
Recombinant Strain ◽  
Antimicrobial Agents ◽  
Low Cost ◽  
Rapid Screening ◽  
Murine Macrophages ◽  
Antimycobacterial Agents

ABSTRACT A reliable and low-cost method that enables rapid screening of the activity exerted by new antimicrobial agents on intracellularly growingMycobacterium avium has been developed. To this aim, a recombinant (lacZ) strain of M. aviumexpressing the Escherichia coli β-galactosidase gene was used to evaluate, in murine macrophages, the susceptibility of M. avium to common antimycobacterial agents. β-Galactosidase levels, measured in the presence of each of the antibiotics tested, were closely correlated with the number of CFU recovered from theM. avium lacZ strain-infected macrophages.

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