Purification and characterization of enzyme responsible for N-myristoylation of octapeptide in aqueous solution without ATP and coenzyme a from Pseudomonas aeruginosa

2006 ◽  
Vol 102 (3) ◽  
pp. 193-197 ◽  
Author(s):  
Takahiro Jyomoto ◽  
Masayuki Azuma ◽  
Nazneen Naher Islam ◽  
Ryo Fujinami ◽  
Toshifumi Takao ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Pseudomonas Aeruginosa ◽  
Coenzyme A ◽  
Purification And Characterization

scholarly journals Purification and Characterization of Pseudomonas aeruginosa PAO1 Asparaginase

2015 ◽  
Vol 28 ◽  
pp. 72-77 ◽  
Author(s):  
Takeshi Kuwabara ◽  
Asep A. Prihanto ◽  
Mamoru Wakayama ◽  
Kazuyoshi Takagi
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Purification And Characterization ◽  
Pseudomonas Aeruginosa Pao1

scholarly journals Purification and characterization of a novel enoyl coenzyme A reductase from Streptomyces collinus.

1992 ◽  
Vol 174 (12) ◽  
pp. 3850-3854 ◽  
Author(s):  
K A Reynolds ◽  
P Wang ◽  
K M Fox ◽  
M K Speedie ◽  
Y Lam ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Purification And Characterization ◽  
Streptomyces Collinus ◽  
Coenzyme A Reductase

Purification and characterization of phosphotriesterases from Pseudomonas aeruginosa F10B and Clavibacter michiganense subsp. insidiosum SBL11

2006 ◽  
Vol 52 (2) ◽  
pp. 157-168 ◽  
Author(s):  
Subhas Das ◽  
Dileep Kumar Singh
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Molecular Mass ◽  
Half Life ◽  
Indoleacetic Acid ◽  
Bacterial Strains ◽  
Purification And Characterization ◽  
Temperature Optimum ◽  
Microbial Biodegradation ◽  
Membrane Bound

A microbial biodegradation of monocrotophos was studied in the present investigation. The monocrotophos-degrading enzyme was purified and characterized from two soil bacterial strains. The cells were disrupted and the membrane-bound fractions were studied for purification and characterization. Solubilization of the membrane-bound fractions released nearly 80% of the bound protein. Phase separation further enriched the enzyme fraction 34–41 times. The enzyme phosphotriesterase (PTE) from both the strains was purified to more than 1000-fold with 13%–16% yield. Purified PTE from Clavibacter michiganense subsp. insidiosum SBL11 is a monomeric enzyme with a molecular mass of 43.5 kDa (pI of 7.5), while PTE from Pseudomonas aeruginosa F10B is a heterodimeric enzyme with a molecular mass of 43 and 41 kDa (pI of 7.9 and 7.35). Both purified enzymes are stable enzymes with peak activity at pH 9.0. The enzyme from strain F10B was more thermostable (half-life = 7.3 h) than that from SBL11 (half-life = 6.4 h at 50 °C), while both showed the same temperature optimum of 37 °C. Inhibitors like dithiothreitol and EDTA inhibited the purified enzyme, while p-chloromercuribenzoic acid and indoleacetic acid had a very little effect.Key words: biodegradation, monocrotophos, phosphotriesterase, Pseudomonas aeruginosa F10B, Clavibacter michiganense subsp. insidiosum SBL11.

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