Co-expression of l-arabinose isomerase and d-glucose isomerase in E. coli and development of an efficient process producing simultaneously d-tagatose and d-fructose

2007 ◽  
Vol 40 (6) ◽  
pp. 1531-1537 ◽  
Author(s):  
Moez Rhimi ◽  
Ezzedine Ben Messaoud ◽  
Mohamed Ali Borgi ◽  
Khalifa Ben khadra ◽  
Samir Bejar
Keyword(s):  
Glucose Isomerase ◽  
E Coli ◽  
Efficient Process ◽  
Arabinose Isomerase

scholarly journals Efficient synthesis of Ibrutinib chiral intermediate in high space-time yield by recombinant E. coli co-expressing alcohol dehydrogenase and glucose dehydrogenase

RSC Advances ◽  
2019 ◽  
Vol 9 (4) ◽  
pp. 2325-2331 ◽  
Author(s):  
Yitong Chen ◽  
Baodi Ma ◽  
Songshuang Cao ◽  
Xiaomei Wu ◽  
Yi Xu
Keyword(s):  
Alcohol Dehydrogenase ◽  
Glucose Dehydrogenase ◽  
Space Time ◽  
Optically Active ◽  
Efficient Synthesis ◽  
E Coli ◽  
Efficient Process ◽  
High Space ◽  
Space Time Yield

A simple and efficient process for the synthesis of optically active (S)-N-boc-3-hydroxy piperidine was developed using the “designer cells” co-expressing alcohol dehydrogenase and glucose dehydrogenase.

Expression, Enzymatic Characterization, and High-Level Production of Glucose Isomerase from Actinoplanes missouriensis CICIM B0118(A) in Escherichia coli

2011 ◽  
Vol 66 (11-12) ◽  
pp. 605-613 ◽  
Author(s):  
He Wang ◽  
Ruijin Yang ◽  
Xiao Hua ◽  
Zhong Zhang ◽  
Wei Zhao ◽  
...  
Keyword(s):  
Ph Value ◽  
Glucose Isomerase ◽  
Medium Composition ◽  
Gene Encoding ◽  
E Coli ◽  
Optimum Ph ◽  
One Step ◽  
Ph Range ◽  
High Level ◽  
Level Production

High-level production of recombinant glucose isomerase (rGI) is desirable for lactulose synthesis. In this study, the xylA gene encoding glucose isomerase from Actinoplanes missouriensis CICIM B0118(A) was cloned and expressed in E. coli BL21(DE3), and high-level production was performed by optimization of the medium composition. rGI was purified from a recombinant E. coli BL21(DE3) and characterized. The optimum pH value of the purified enzyme was 8.0 and it was relatively stable within the pH range of 7.0 - 9.0. Its optimum temperature was around 85 °C, and it exhibited good thermostability when the temperature was lower than 90 °C. The maximum enzyme activity required the presence of both Co2+ and Mg2+, at the concentrations of 200 μM and 8 mM, respectively. With high-level expression and the simple one-step chromatographic purification of the His-tagged recombinant enzyme, this GI could be used in industrial production of lactulose as a potential economic tool

scholarly journals d-Xylose (d-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728. Gene cloning, sequence and expression

1991 ◽  
Vol 277 (1) ◽  
pp. 263-271 ◽  
Author(s):  
T Loviny-Anderton ◽  
P C Shaw ◽  
M K Shin ◽  
B S Hartley
Keyword(s):  
Sequence Similarity ◽  
Shuttle Vector ◽  
Xylose Isomerase ◽  
Glucose Isomerase ◽  
Open Reading Frame ◽  
Reading Frame ◽  
E Coli ◽  
Ribosome Binding ◽  
Arthrobacter Strain ◽  
Cloned Gene

Arthrobacter strain N.R.R.L. B3728 superproduces a D-xylose isomerase that is also a useful industrial D-glucose isomerase. The gene (xylA) that encodes it has been cloned by complementing a xylA mutant of the ancestral strain, with the use of a shuttle vector. The 5′ region shows strong sequence similarity to Escherichia coli consensus promoters and ribosome-binding sequences and allows high levels of expression in E. coli. The coding sequence shows similarity to those for other D-xylose isomerases and is followed by 22 nucleotide residues with stop codons in each reading frame, a good ‘consensus’ ribosome-binding site and an open reading frame showing similarity to those of known D-xylulokinases (xylB). Studies on the expression of the cloned gene in Arthrobacter and in E. coli suggest that the two genes are part of a xyl operon regulated by a repressor that is defective in strain B3728. Codon usage in these two genes, and in another open reading frame (nxi) that was adventitiously isolated during early cloning attempts, shows some characteristic omissions and a strong G + C preference in redundant positions.

Expression and translocation of glucose isomerase as a fusion protein in E. coli

2004 ◽  
Vol 35 (2-3) ◽  
pp. 105-112 ◽  
Author(s):  
Berna Sarıyar ◽  
Pınar Özkan ◽  
Betül Kırdar ◽  
Amable Hortaçsu
Keyword(s):  
Fusion Protein ◽  
Glucose Isomerase ◽  
E Coli

scholarly journals Multi-Enzymsystem zur Herstellung eines alternativen Zuckersirups

BIOspektrum ◽  
2020 ◽  
Vol 26 (6) ◽  
pp. 679-681
Author(s):  
Sabine Lutz-Wahl ◽  
Eva Pross ◽  
Jörg Hinrichs ◽  
Lutz Fischer
Keyword(s):  
Sugar Content ◽  
Glucose Isomerase ◽  
Overweight People ◽  
Sugar Syrup ◽  
Sugar Mixture ◽  
Arabinose Isomerase

Abstract Energy-rich foods lead to an increase of overweight people in our societies. Mainly the fat and sugar content in foods is responsible for this progress. However, both components are very important for the taste and acceptance of foods. Thus, the abundant available lactose will be enzymatically modified by using the enzymes β-galactosidase, L-arabinose isomerase and glucose isomerase in order to generate a new natural sugar syrup. The new sugar mixture will be much sweeter than lactose.

Endotoxin Alteration of the Mucopolysaccharide Blood Vessel Coating in Rats

1974 ◽  
Vol 32 ◽  
pp. 148-149
Author(s):  
D. E. Philpott ◽  
A. Takahashi
Keyword(s):  
Skeletal Muscle ◽  
Endothelial Cells ◽  
Salivary Gland ◽  
Carotid Artery ◽  
Basement Membrane ◽  
Coronary Vessels ◽  
Ruthenium Red ◽  
E Coli ◽  
Old Rats ◽  
The Brain

Two month, eight month and two year old rats were treated with 10 or 20 mg/kg of E. Coli endotoxin I. P. The eight month old rats proved most resistant to the endotoxin. During fixation the aorta, carotid artery, basil arartery of the brain, coronary vessels of the heart, inner surfaces of the heart chambers, heart and skeletal muscle, lung, liver, kidney, spleen, brain, retina, trachae, intestine, salivary gland, adrenal gland and gingiva were treated with ruthenium red or alcian blue to preserve the mucopolysaccharide (MPS) coating. Five, 8 and 24 hrs of endotoxin treatment produced increasingly marked capillary damage, disappearance of the MPS coating, edema, destruction of endothelial cells and damage to the basement membrane in the liver, kidney and lung.

Ribosome Structural Organization

1974 ◽  
Vol 32 ◽  
pp. 332-333
Author(s):  
James A. Lake
Keyword(s):  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Small Subunit ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Specific Antibodies ◽  
X Ray ◽  
E Coli ◽  
Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

Sites of Adsorption of the Bacteriophages T3 and T5 on the Wall of Escherichia Coli B.

1967 ◽  
Vol 25 ◽  
pp. 96-97
Author(s):  
Manfred E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Electron Microscope ◽  
Uranyl Acetate ◽  
E Coli ◽  
Receptor Sites ◽  
Rigid Cell Wall ◽  
Host Cell Surface ◽  
Bacterial Viruses ◽  
Escherichia Coli B

Bacterial viruses adsorb specifically to receptors on the host cell surface. Although the chemical composition of some of the cell wall receptors for bacteriophages of the T-series has been described and the number of receptor sites has been estimated to be 150 to 300 per E. coli cell, the localization of the sites on the bacterial wall has been unknown.When logarithmically growing cells of E. coli are transferred into a medium containing 20% sucrose, the cells plasmolize: the protoplast shrinks and becomes separated from the somewhat rigid cell wall. When these cells are fixed in 8% Formaldehyde, post-fixed in OsO4/uranyl acetate, embedded in Vestopal W, then cut in an ultramicrotome and observed with the electron microscope, the separation of protoplast and wall becomes clearly visible, (Fig. 1, 2). At a number of locations however, the protoplasmic membrane adheres to the wall even under the considerable pull of the shrinking protoplast. Thus numerous connecting bridges are maintained between protoplast and cell wall. Estimations of the total number of such wall/membrane associations yield a number of about 300 per cell.

Emigration of neutrophils in the central nervous system

1983 ◽  
Vol 41 ◽  
pp. 788-789
Author(s):  
John L.Beggs ◽  
John D. Waggener ◽  
Wanda Miller ◽  
Jane Watkins
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Osmium Tetroxide ◽  
White Blood Cells ◽  
Arterial Perfusion ◽  
E Coli ◽  
Intracisternal Injection ◽  
The Central Nervous System ◽  
Brain And Spinal Cord ◽  
Interendothelial Junctions

Studies using mesenteric and ear chamber preparations have shown that interendothelial junctions provide the route for neutrophil emigration during inflammation. The term emigration refers to the passage of white blood cells across the endothelium from the vascular lumen. Although the precise pathway of transendo- thelial emigration in the central nervous system (CNS) has not been resolved, the presence of different physiological and morphological (tight junctions) properties of CNS endothelium may dictate alternate emigration pathways.To study neutrophil emigration in the CNS, we induced meningitis in guinea pigs by intracisternal injection of E. coli bacteria.In this model, leptomeningeal inflammation is well developed by 3 hr. After 3 1/2 hr, animals were sacrificed by arterial perfusion with 3% phosphate buffered glutaraldehyde. Tissues from brain and spinal cord were post-fixed in 1% osmium tetroxide, dehydrated in alcohols and propylene oxide, and embedded in Epon. Thin serial sections were cut with diamond knives and examined in a Philips 300 electron microscope.

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