scholarly journals Erratum to: Efficient production of active form of recombinant cassava hydroxynitrile lyase using Escherichia coli in low-temperature culture

2008 ◽  
Vol 80 (4) ◽  
pp. 747-748
Author(s):  
Hisashi Semba ◽  
Eita Ichige ◽  
Tadayuki Imanaka ◽  
Haruyuki Atomi ◽  
Hideki Aoyagi
Keyword(s):  
Escherichia Coli ◽  
Low Temperature ◽  
Active Form ◽  
Efficient Production ◽  
Hydroxynitrile Lyase

Efficient Production of Active Form Recombinant Cassava Hydroxynitrile Lyase Using Escherichia coli in Low-Temperature Culture

2010 ◽  
pp. 133-144 ◽  
Author(s):  
Hisashi Semba ◽  
Eita Ichige ◽  
Tadayuki Imanaka ◽  
Haruyuki Atomi ◽  
Hideki Aoyagi
Keyword(s):  
Escherichia Coli ◽  
Low Temperature ◽  
Active Form ◽  
Efficient Production ◽  
Hydroxynitrile Lyase

Efficient production of active form of recombinant cassava hydroxynitrile lyase using Escherichia coli in low-temperature culture

2008 ◽  
Vol 79 (4) ◽  
pp. 563-569 ◽  
Author(s):  
Hisashi Semba ◽  
Eita Ichige ◽  
Tadayuki Imanaka ◽  
Haruyuki Atomi ◽  
Hideki Aoyagi
Keyword(s):  
Escherichia Coli ◽  
Low Temperature ◽  
Active Form ◽  
Efficient Production ◽  
Hydroxynitrile Lyase

scholarly journals Efficient Production of l-Ribose with a Recombinant Escherichia coli Biocatalyst

2008 ◽  
Vol 74 (10) ◽  
pp. 2967-2975 ◽  
Author(s):  
Ryan D. Woodyer ◽  
Nathan J. Wymer ◽  
F. Michael Racine ◽  
Shama N. Khan ◽  
Badal C. Saha
Keyword(s):  
Escherichia Coli ◽  
Large Scale ◽  
Active Form ◽  
Apium Graveolens ◽  
Efficient Production ◽  
Scale Production ◽  
Gene Encoding ◽  
Large Scale Production ◽  
One Step ◽  
Rare Sugars

ABSTRACT A new synthetic platform with potential for the production of several rare sugars, with l-ribose as the model target, is described. The gene encoding the unique NAD-dependent mannitol-1-dehydrogenase (MDH) from Apium graveolens (garden celery) was synthetically constructed for optimal expression in Escherichia coli. This MDH enzyme catalyzes the interconversion of several polyols and their l-sugar counterparts, including the conversion of ribitol to l-ribose. Expression of recombinant MDH in the active form was successfully achieved, and one-step purification was demonstrated. Using the created recombinant E. coli strain as a whole-cell catalyst, the synthetic utility was demonstrated for production of l-ribose, and the system was improved using shaken flask experiments. It was determined that addition of 50 to 500 μM ZnCl2 and addition of 5 g/liter glycerol both improved production. The final levels of conversion achieved were >70% at a concentration of 40 g/liter and >50% at a concentration of 100 g/liter. The best conditions determined were then scaled up to a 1-liter fermentation that resulted in 55% conversion of 100 g/liter ribitol in 72 h, for a volumetric productivity of 17.4 g liter−1 day−1. This system represents a significantly improved method for the large-scale production of l-ribose.

scholarly journals Efficient production of active chicken avidin using a bacterial signal peptide in Escherichia coli

2004 ◽  
Vol 384 (2) ◽  
pp. 385-390 ◽  
Author(s):  
Vesa P. HYTÖNEN ◽  
Olli H. LAITINEN ◽  
Tomi T. AIRENNE ◽  
Heidi KIDRON ◽  
Niko J. MELTOLA ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Signal Sequence ◽  
Specific Binding ◽  
Affinity Purification ◽  
Active Form ◽  
Efficient Production ◽  
E Coli ◽  
Secretion Signal ◽  
Technology Applications ◽  
Biotin Binding

Chicken avidin is a highly popular tool with countless applications in the life sciences. In the present study, an efficient method for producing avidin protein in the periplasmic space of Escherichia coli in the active form is described. Avidin was produced by replacing the native signal sequence of the protein with a bacterial OmpA secretion signal. The yield after a single 2-iminobiotin–agarose affinity purification step was approx. 10 mg/l of virtually pure avidin. Purified avidin had 3.7 free biotin-binding sites per tetramer and showed the same biotin-binding affinity and thermal stability as egg-white avidin. Avidin crystallized under various conditions, which will enable X-ray crystallographic studies. Avidin produced in E. coli lacks the carbohydrate chains of chicken avidin and the absence of glycosylation should decrease the non-specific binding that avidin exhibits towards many materials [Rosebrough and Hartley (1996) J. Nucl. Med. 37, 1380–1384]. The present method provides a feasible and inexpensive alternative for the production of recombinant avidin, avidin mutants and avidin fusion proteins for novel avidin–biotin technology applications.

Flux redistribution of central carbon metabolism for efficient production of L‐tryptophan in Escherichia coli

2021 ◽  
Author(s):  
Bo Xiong ◽  
Yongduo Zhu ◽  
Daoguang Tian ◽  
Shuai Jiang ◽  
Xiaoguang Fan ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Carbon Metabolism ◽  
Central Carbon Metabolism ◽  
Efficient Production ◽  
Central Carbon ◽  
Flux Redistribution

Continuous low-temperature spray drying approach for efficient production of high quality native rice starch

2021 ◽  
pp. 1-16
Author(s):  
Jamie Boon Jun Tay ◽  
Xinying Chua ◽  
Cailing Ang ◽  
Kelvin Kim Tha Goh ◽  
Gomathy Sandhya Subramanian ◽  
...  
Keyword(s):  
Low Temperature ◽  
Spray Drying ◽  
Rice Starch ◽  
Efficient Production ◽  
High Quality

Inactivation of Escherichia coli by microwave induced low temperature argon plasma treatments

2002 ◽  
Vol 53 (4) ◽  
pp. 341-346 ◽  
Author(s):  
Dambadarjaa Purevdorj ◽  
Noriyuki Igura ◽  
Isao Hayakawa ◽  
Osamu Ariyada
Keyword(s):  
Escherichia Coli ◽  
Low Temperature ◽  
Argon Plasma ◽  
Plasma Treatments

Optimized Culture Conditions for the Efficient Production of Porcine Adenylate Kinase in Recombinant Escherichia coli

2010 ◽  
Vol 162 (3) ◽  
pp. 823-829 ◽  
Author(s):  
Toru Matsui ◽  
Takashi Togari ◽  
Satoru Misawa ◽  
Tomoyuki Namihira ◽  
Naoya Shinzato ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Adenylate Kinase ◽  
Culture Conditions ◽  
Recombinant Escherichia Coli ◽  
Efficient Production
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