1625 Expression and purification of a novel bacterial expansin from Bacillus subtilis that synergistically degrades cellulose with fibrolytic enzymes

2016 ◽  
Vol 94 (suppl_5) ◽  
pp. 791-791
Author(s):  
A. A. P. Cervantes ◽  
I. Muhammad ◽  
C. F. Gonzalez ◽  
D. Vyas ◽  
A. T. Adesogan
Keyword(s):  
Bacillus Subtilis ◽  
Expression And Purification ◽  
Fibrolytic Enzymes ◽  
Bacterial Expansin

scholarly journals Expression and purification of untagged and histidine-tagged folate-dependent tRNA:m5U54 methyltransferase from Bacillus subtilis

2010 ◽  
Vol 73 (1) ◽  
pp. 83-89 ◽  
Author(s):  
Djemel Hamdane ◽  
Stéphane Skouloubris ◽  
Hannu Myllykallio ◽  
Béatrice Golinelli-Pimpaneau
Keyword(s):  
Bacillus Subtilis ◽  
Expression And Purification

Gene cloning and characterization of glycine oxidase from newly isolated Bacillus subtilis strain R5

Biologia ◽  
2011 ◽  
Vol 66 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Farrukh Jamil ◽  
Naeem Rashid ◽  
Qurra-tul-Ann Gardner ◽  
Muhammad Akhtar
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Specific Activity ◽  
Subtilis Strain ◽  
Amino Acid Residues ◽  
Expression And Purification ◽  
Gene Encoding ◽  
Glycine Oxidase ◽  
Bacillus Subtilis Strain R5

AbstractThe gene encoding the glycine oxidase from Bacillus subtilis strain R5 (goxR) was cloned and expressed in Escherichia coli. The gene consisted of 1,110 nucleotides that encoded a protein (GoxR) of 369 amino acid residues with a molecular mass of 40,761 Da. The GoxR exhibited 98.6% identity with glycine oxidase from B. subtilis strain 168. Gene expression and purification of the recombinant GoxR were performed. The recombinant GoxR existed in a homotetramer form. The recombinant protein effectively catalyzed the oxidation of glycine and d-alanine. The specific activity of the purified recombinant GoxR was 0.96 U/mg when glycine was used as a substrate and 1.0 U/mg when d-alanine was substrate. The enzyme displayed its highest activity at pH 8.0 and at a temperature of 50°C. The activation energy of the reaction catalyzed by the enzyme was calculated to be 26 kJ/mol. The enzyme activity was significantly inhibited in the presence of organic solvents. No enhancement of enzyme activity was observed in the presence of metal cations. The experimental results presented in this study demonstrate that the enzyme was a bonafide glycine oxidase.

Heterologous expression and purification of protopectinase-N from Bacillus subtilis in Pichia pastoris

2006 ◽  
Vol 41 (4) ◽  
pp. 975-979 ◽  
Author(s):  
Zhan-Min Liu ◽  
Zhao-Xin Lu ◽  
Feng-Xia Lv ◽  
Xiao-Mei Bie ◽  
Hai-Zhen Zhao
Keyword(s):  
Bacillus Subtilis ◽  
Pichia Pastoris ◽  
Heterologous Expression ◽  
Expression And Purification

Expression and Purification of Extracellular Penicillin G Acylase in Bacillus subtilis

2001 ◽  
Vol 21 (1) ◽  
pp. 60-64 ◽  
Author(s):  
Sheng Yang ◽  
He Huang ◽  
Ruan Zhang ◽  
Xiaodong Huang ◽  
Shiyun Li ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Expression And Purification

Use of Antibody to aid Visualization of Protein at the Termini of Bacteriophage Ø29 DNA

1980 ◽  
Vol 38 ◽  
pp. 540-541
Author(s):  
Dwight Anderson ◽  
Charlene Peterson ◽  
Gursaran Notani ◽  
Bernard Reilly
Keyword(s):  
Electron Microscopy ◽  
Bacillus Subtilis ◽  
Dna Synthesis ◽  
Restriction Endonuclease ◽  
Protein Complex ◽  
Protein Product ◽  
Viral Dna ◽  
Small Proteins ◽  
Antibody Labeling ◽  
Subtilis Bacteriophage

The protein product of cistron 3 of Bacillus subtilis bacteriophage Ø29 is essential for viral DNA synthesis and is covalently bound to the 5’-termini of the Ø29 DNA. When the DNA-protein complex is cleaved with a restriction endonuclease, the protein is bound to the two terminal fragments. The 28,000 dalton protein can be visualized by electron microscopy as a small dot and often is seen only when two ends are in apposition as in multimers or in glutaraldehyde-fixed aggregates. We sought to improve the visibility of these small proteins by use of antibody labeling.

Antibacterial activity of Celastrol against Bacillus subtilis

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
N Padilla-Montaño ◽  
IL Bazzocchi ◽  
L Moujir
Keyword(s):  
Antibacterial Activity ◽  
Bacillus Subtilis

Mikrobizide und viruzide Aufbereitung von Dialysegeräten

2018 ◽  
Vol 22 (02) ◽  
pp. 82-89
Author(s):  
Friedrich von Rheinbaben ◽  
Oliver Riebe ◽  
Johanna Köhnlein ◽  
Sebastian Werner
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Bacillus Subtilis ◽  
Phase 3 ◽  
Aspergillus Brasiliensis

ZusammenfassungZentrales Bauteil des Genius® 90 Therapie Systems ist der sogenannte Genius-Tank, dem die frische Dialyseflüssigkeit entnommen und in den die verbrauchte Lösung nach der Dialyse zurückgeführt wird. Daher kommt der sicheren Aufbereitung des Systems eine besondere Bedeutung zu. Hierfür wird ein Aufbereitungsverfahren unter Verwendung von UV-Licht in Kombination mit einem chemischen Desinfektionsmittel angewendet. Ziel der hier beschriebenen Untersuchung war es, die Wirkungsbreite und Wirkungstiefe dieses Aufbereitungsverfahrens unter praxisnahen Phase-3-Bedingungen zu ermitteln. Dazu wurde das Gerät mit Mikroorganismen und Viren künstlich kontaminiert und die Wirkung der einzelnen Verfahrensschritte ermittelt. Im Gegensatz zu der üblichen Vorgehensweise praxisnaher Untersuchungen machen Aufbereitungsverfahren medizinischer Geräte unter Phase-3-Kriterien meist eine neuartige Arbeitsweise erforderlich – im Falle der hier vorgestellten Untersuchung sogar die Konstruktion eines speziellen Geräts zur Platzierung von Keimträgen im Genius-Tank. Im Ergebnis konnte gezeigt werden, dass bereits UV-Licht allein sowie in Kombination mit einem chemischen Desinfektionsmittel unter praxisnahen Bedingungen eine sichere Wirksamkeit gegen Bakterien (Pseudomonas aeruginosa) und bakterielle Sporen (Bacillus subtilis), Schimmelpilze (Aspergillus brasiliensis) und Viren (Murines Parvovirus) besitzt.

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