Purification and characterization of an alkaline protease from Pseudomonas aeruginosa MN1

Bayoudh, Ahmed; Gharsallah, Néji; Chamkha, Mohamed; Dhouib, Abdelhafidh; Ammar, Slim Ben; Nasri, Mohammad

doi:10.1038/sj.jim.2900822

Cited by 51 publications

(40 citation statements)

References 8 publications

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“…3). These reports are in accordance with previous findings that the optimum pH of 8.0 was obtained from A. parasiticus [17], A. fumigatus [32], Pseudomonas aeruginosa MN1 [35]. Some other investigators have also reported high levels of alkaline protease from pH 11 to 12 [23,36].…”

Section: Effect Of Ph On Enzyme Activity and Stabilitysupporting

confidence: 92%

Purification, characterization and crystallization of an extracellular alkaline protease from Aspergillus nidulans HA‐10

Charles

Devanathan

Anbu

et al. 2008

J. Basic Microbiol.

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Aspergillus nidulans is a highly potent fungus used in the production of alkaline protease. Extracellular alkaline protease was purified from A. nidulans in a two-step procedure involving ammonium sulphate precipitation and Sephadex G-100 column chromatography. The molecular mass of the enzyme was determined to be 42 kDa by SDS-PAGE. The enzyme activity was also analyzed by zymogram with gelatin. The enzyme was more stable over a wide range of pH (6-10) and the temperatures up to 50 degrees C. It showed optimum enzyme activity at pH 8.0 and a temperature of 35 degrees C. The protease enzyme was completely inhibited by the serine protease inhibitor of phenylmethylsulfonyl fluoride (PMSF). The crystallization of the purified enzyme was performed by hanging drop vapour diffusion method using PEG 6000 as the precipitant. The micro crystals occurred in 40% of PEG 6,000.

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Section: Effect Of Ph On Enzyme Activity and Stabilitysupporting

confidence: 92%

Purification, characterization and crystallization of an extracellular alkaline protease from Aspergillus nidulans HA‐10

Charles

Devanathan

Anbu

et al. 2008

J. Basic Microbiol.

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“…A few bacterial groups, such as Pseudomonas, Bacillus (Mabrouk et al 1999;Mehrotra et al 1999;Bayoudh et al 2000) are considered as potent producers for commercial purposes. The microbial proteases are the most significant and can be produced in large quantities; and genetic manipulation of the microbial proteases, which has been used to increase activity, is easier than that for plant and animal proteases (Laxman et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Production of alkaline protease from a newly isolated Exiguobacterium profundum BK-P23 evaluated using the response surface methodology

2013

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Protease producing bacteria were isolated from soil in South Korea. These bacteria were screened in skim milk agar medium using skim milk as the substrate. The highest clear zone producing bacterial strain (BK-P23) was selected for further optimization studies. The strain was identified as Exiguobacterium profundum BK-P23 based on morphological, biochemical and molecular characterizations. The results of the 16S rRNA analysis showed that this strain was highly similar to E. profundum. The strain was able to grow under alkaline conditions at pH 8.5 and a temperature of 30In the preliminary optimization experiments, five different parameters, i.e. carbon source (lactose), nitrogen source (corn steep solid), pH, temperature and incubation period were varied with the goal of optimizing enzyme production in low cost medium using the Box-Behnken design combined with response surface methodology. The optimal conditions were determined to be pH 9.0, a temperature of 30• C, lactose (1.0%) as the carbon source and corn steep solid (1.0%) as the cheap additional nitrogen source. In addition, 24 h of incubation was shown to produce the highest protease yield. Overall, the amount of enzyme produced was significantly higher in the optimized medium when compared with the original medium.

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“…These catalyze total hydrolysis of proteins and specifically act on interior peptide bonds (Bayoudh et al 2000).…”

Section: Introductionmentioning

confidence: 99%

Fibrinolytic Bacterial Enzymes with Thrombolytic Activity

Kotb¹

2012

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Purification and characterization of an alkaline protease from Pseudomonas aeruginosa MN1

Cited by 51 publications

References 8 publications

Purification, characterization and crystallization of an extracellular alkaline protease from Aspergillus nidulans HA‐10

Purification, characterization and crystallization of an extracellular alkaline protease from Aspergillus nidulans HA‐10

Production of alkaline protease from a newly isolated Exiguobacterium profundum BK-P23 evaluated using the response surface methodology

Fibrinolytic Bacterial Enzymes with Thrombolytic Activity

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