scholarly journals Characterization of an Aldehyde Oxidoreductase From the Mesophilic Bacterium Aromatoleum aromaticum EbN1, a Member of a New Subfamily of Tungsten-Containing Enzymes

2019 ◽  
Vol 10 ◽  
Author(s):  
Fabian Arndt ◽  
Georg Schmitt ◽  
Agnieszka Winiarska ◽  
Martin Saft ◽  
Andreas Seubert ◽  
...  
Keyword(s):  
Aldehyde Oxidoreductase ◽  
Mesophilic Bacterium

Characterization of a thermostable endoglucanase from Cellulomonas fimi ATCC484

2018 ◽  
Vol 96 (1) ◽  
pp. 68-76 ◽  
Author(s):  
Hirak Saxena ◽  
Bryan Hsu ◽  
Marc de Asis ◽  
Mirko Zierke ◽  
Lyann Sim ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Hydrolytic Activity ◽  
Carbohydrate Binding ◽  
Cell Wall Polysaccharides ◽  
Cellulomonas Fimi ◽  
Thermal Denaturation Temperature ◽  
Mesophilic Bacterium

Bacteria in the genus Cellulomonas are well known as secretors of a variety of mesophilic carbohydrate degrading enzymes (e.g., cellulases and hemicellulases), active against plant cell wall polysaccharides. Recent proteomic analysis of the mesophilic bacterium Cellulomonas fimi ATCC484 revealed uncharacterized enzymes for the hydrolysis of plant cell wall biomass. Celf_1230 (CfCel6C), a secreted protein of Cellulomonas fimi ATCC484, is a novel member of the GH6 family of cellulases that could be successfully expressed in Escherichia coli. This enzyme displayed very little enzymatic/hydrolytic activity at 30 °C, but showed an optimal activity around 65 °C, and exhibited a thermal denaturation temperature of 74 °C. In addition, it also strongly bound to filter paper despite having no recognizable carbohydrate binding module. Our experiments show that CfCel6C is a thermostable endoglucanase with activity on a variety of β-glucans produced by an organism that struggles to grow above 30 °C.

Biochemical and spectroscopic characterization of an aldehyde oxidoreductase isolated from Desulfovibrio aminophilus

2006 ◽  
Vol 100 (1) ◽  
pp. 44-50 ◽  
Author(s):  
Anders Thapper ◽  
Maria G. Rivas ◽  
Carlos D. Brondino ◽  
Bernard Ollivier ◽  
Guy Fauque ◽  
...  
Keyword(s):  
Spectroscopic Characterization ◽  
Aldehyde Oxidoreductase

scholarly journals Isolation and characterization of isocitrate lyase from a thermophilic Bacillus sp

1978 ◽  
Vol 173 (1) ◽  
pp. 165-177 ◽  
Author(s):  
R M Chell ◽  
T K Sundaram ◽  
A E Wilkinson
Keyword(s):  
Thermal Denaturation ◽  
Isocitrate Lyase ◽  
Homogeneous State ◽  
Thiol Groups ◽  
Thermophilic Bacillus ◽  
Relative Paucity ◽  
Salt Activation ◽  
Isolation And Characterization ◽  
Mesophilic Bacterium

Isocitrate lyase was isolated in homogeneous state from a thermophilic Bacillus. The enzyme has a mol.wt. of 180000 and a pI of 4.5 and contains threonine as the N-terminal residue. It resembles in size the cognate enzyme from the mesophilic bacterium Pseudomonas indigofera, but is smaller than the enzyme from the eukaryotic fungus Neurospora crassa. All three lyases are tetramers and similar in amino acid composition, but the thermophile enzyme is distinctive from its mesophilic coutnerparts in possessing a lower catalytic-centre activity, greater resistance to chemical and thermal denaturation and fewer thiol groups and in being strongly activated by salts. Salt activation, by 0.4M-KCl, is about 3-fold at 30 degrees C and pH 6.8 and weakens progressively as the temperature or pH is raised. The activation is probably due to a change in the enzyme conformation caused by the electrolyte modifying the interaction between charged groups or between hydrophobic groups in protein. The possible significance of the salt activation, of the relative paucity of thiol groups and of the greater resistance to chemical denaturants is discussed. Besides its effect on the Vmax., KCl produces large increases in the magnitude of several kinetic parameters. A rise in reaction temperature from 30 to 55 degrees C produces a somewhat similar result. In view of these peculiar features, the patterns of inhibition of enzyme activity by compounds such as succinate and phosphoenolpyruvate were examined at 30 and 55 degrees C in the presence and absence of KCl.

scholarly journals DNA-guided DNA cleavage at moderate temperatures by Clostridium butyricum Argonaute

2019 ◽  
Author(s):  
Jorrit W. Hegge ◽  
Daan C. Swarts ◽  
Stanley D. Chandradoss ◽  
Tao Ju Cui ◽  
Jeroen Kneppers ◽  
...  
Keyword(s):  
Host Defense ◽  
Dna Cleavage ◽  
Elevated Temperatures ◽  
Clostridium Butyricum ◽  
Dna Targeting ◽  
Dna Cleaving ◽  
Double Stranded Dna ◽  
Argonaute Proteins ◽  
Mesophilic Bacterium

AbstractProkaryotic Argonaute proteins (pAgos) constitute a diverse group of endonucleases of which some mediate host defense by utilizing small interfering DNA guides (siDNA) to cleave complementary invading DNA. This activity can be repurposed for programmable DNA cleavage. However, currently characterized DNA-cleaving pAgos require elevated temperatures (≥65°C) for their activity, making them less suitable for applications that require moderate temperatures, such as genome editing. Here we report the functional and structural characterization of the siDNA-guided DNA-targeting pAgo from the mesophilic bacterium Clostridium butyricum (CbAgo). CbAgo displays a preference for siDNAs that have a deoxyadenosine at the 5’-end and thymidines in the sub-seed segment (siDNA nucleotides 2-4). Furthermore, CbAgo mediates DNA-guided DNA cleavage of AT-rich double stranded DNA at moderate temperatures (37°C). This study demonstrates that certain pAgos are capable of programmable DNA cleavage at moderate temperatures and thereby expands the scope of the potential pAgo–based applications.

scholarly journals Nocardia sp. Carboxylic Acid Reductase: Cloning, Expression, and Characterization of a New Aldehyde Oxidoreductase Family

2004 ◽  
Vol 70 (3) ◽  
pp. 1874-1881 ◽  
Author(s):  
Aimin He ◽  
Tao Li ◽  
Lacy Daniels ◽  
Ian Fotheringham ◽  
John P. N. Rosazza
Keyword(s):  
Carboxylic Acid ◽  
Gene Family ◽  
Carboxylic Acids ◽  
Affinity Tag ◽  
Aldehyde Oxidoreductase ◽  
Nocardia Sp ◽  
New Gene ◽  
Ferulic Acids

ABSTRACT We have cloned, sequenced, and expressed the gene for a unique ATP- and NADPH-dependent carboxylic acid reductase (CAR) from a Nocardia species that reduces carboxylic acids to their corresponding aldehydes. Recombinant CAR containing an N-terminal histidine affinity tag had Km values for benzoate, ATP, and NADPH that were similar to those for natural CAR, and recombinant CAR reduced benzoic, vanillic, and ferulic acids to their corresponding aldehydes. car is the first example of a new gene family encoding oxidoreductases with remote acyl adenylation and reductase sites.

Characterization of a poly(butylene adipate- co -terephthalate) hydrolase from the aerobic mesophilic bacterium Bacillus pumilus

2017 ◽  
Vol 137 ◽  
pp. 11-22 ◽  
Author(s):  
Fumihiro Muroi ◽  
Yuya Tachibana ◽  
Phouvilay Soulenthone ◽  
Kiriko Yamamoto ◽  
Tsukasa Mizuno ◽  
...  
Keyword(s):  
Bacillus Pumilus ◽  
Mesophilic Bacterium ◽  
Bacterium Bacillus

Morphological Characterization of Mycobacteriophage R1

1974 ◽  
Vol 32 ◽  
pp. 254-255
Author(s):  
B. L. Soloff ◽  
T. A. Rado
Keyword(s):  
Carbon Source ◽  
Stationary Phase ◽  
Growth Phase ◽  
Minimal Medium ◽  
Morphological Characterization ◽  
Logarithmic Growth Phase ◽  
Complete Lysis ◽  
Lysogenic Culture ◽  
Logarithmic Growth

Mycobacteriophage R1 was originally isolated from a lysogenic culture of M. butyricum. The virus was propagated on a leucine-requiring derivative of M. smegmatis, 607 leu−, isolated by nitrosoguanidine mutagenesis of typestrain ATCC 607. Growth was accomplished in a minimal medium containing glycerol and glucose as carbon source and enriched by the addition of 80 μg/ ml L-leucine. Bacteria in early logarithmic growth phase were infected with virus at a multiplicity of 5, and incubated with aeration for 8 hours. The partially lysed suspension was diluted 1:10 in growth medium and incubated for a further 8 hours. This permitted stationary phase cells to re-enter logarithmic growth and resulted in complete lysis of the culture.

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