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1

Three Pseudomonas aeruginosa strains with different protease profiles

100%

Andrejko M. , Zdybicka-Barabas A. , Janczarek M. , Cytryńska M.

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nr 1

83-90

EN

The proteolytic activity of three Pseudomonas aeruginosa strains, ATCC 27853 - a reference strain, and two clinical isolates was tested. The activity was examined after culturing the bacteria in two different growth media: the minimal M9 medium and rich Luria-Bertani broth (LB). Based on zymograms and protease activity specific assays, it was concluded that the reference strain produced three proteolytic enzymes in the LB medium: protease IV, elastase B and elastase A, while alkaline protease was only produced in the M9 medium. The clinical isolates of P. aeruginosa produced elastase B and alkaline protease when grown in the LB medium and the minimal M9 medium, respectively. PCR analysis confirmed the presence of both the lasB gene encoding elastase B and aprA coding for alkaline protease in the genomes of the three P. aeruginosa strains analyzed. The expression of these genes coding for two important P. aeruginosa virulence factors was dependent on the growth conditions in all the strains studied. The contribution of the extracellular proteinases to the virulence of P. aeruginosa strains used in this study was investigated using an insect model, the greater wax moth Galleria mellonella.

2

Effect of physical and chemical factors in production of alkaline protease enzyme by Bacillus strains

100%

Tebyanian H. , Mirhosseiny S. H. , Bakhtiari A. , Karami A. , Dadseresht S. , Otroshi B.

International Letters of Natural Sciences

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2018

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tom 71

EN

Proteases is family of enzymes and it has crucial role due to their physiological roles and very valuable commercial applications. Alkaline protease are produced by Bacillus species are particular importance because of their thermal stability and stability at different pH values. This study aimed to investigate the effect of physical and chemical factors in production of alkaline protease enzyme fermentation by members of the genus Bacillus. In this study, alkaline protease enzyme production were evaluated in submerged fermentation by Bacillus strains which were isolated from alkaline soils of Guilan province. Factors incubation were optimized such as time, pH, amount of inoculation and ammonium sulfate in alkaline protease enzyme production whit using response surface methodology (RSM) in culture. The maximum enzymatic activity was observed in incubation time of 36 hours, pH=9, inoculation amount of 15% (V) and ammonium sulfate 1.5% (W/V). Factors had significant effect on the production of alkaline protease enzyme such as pH and ammonium sulfate.

3

A novel alkaline protease with antiproliferative activity from fresh fruiting bodies of the toxic wild mushroom Amanita farinosa

100%

Sun J. , Zhao Y. , Chai H. , Wang H. , Ng T. B.

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nr 4

567-572

EN

A novel protease with a molecular mass of 15 kDa was purified from fresh fruiting bodies of the wild mushroom Amanita farinosa. The purification protocol entailed anion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, cation exchange chromatography on SP-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The protease was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and SP-Sepharose. It demonstrated a single 15-kDa band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS/PAGE) and a 15-kDa peak in gel filtration. The optimal pH and optimal temperature of the protease were pH 8.0 and 65 °C, respectively. Proliferation of human hepatoma HepG2 cells was inhibited by the protease with an IC50 of 25 µM. The protease did not have antifungal or ribonuclease activity.

4

A novel alkaline protease with antiproliferative activity from fresh fruiting bodies of the toxic wild mushroom Amanita farinosa

84%

Sun J. , Zhao Y. , Chai H. , Wang H. , Ng T. B.

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nr 4

EN

A novel protease with a molecular mass of 15 kDa was purified from fresh fruiting bodies of the wild mushroom Amanita farinosa. The purification protocol entailed anion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, cation exchange chromatography on SP-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The protease was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and SP-Sepharose. It demonstrated a single 15-kDa band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS/PAGE) and a 15-kDa peak in gel filtration. The optimal pH and optimal temperature of the protease were pH 8.0 and 65 °C, respectively. Proliferation of human hepatoma HepG2 cells was inhibited by the protease with an IC50 of 25 µM. The protease did not have antifungal or ribonuclease activity.

5

Optimization and production of alkaline proteases from agro byproducts using a novel Trichoderma viridiae strain VPG 12, isolated from agro soil

84%

Shivasharanappa K. , Hanchinalmath J. V. , Sundeep Y. S. , Borah D. , Prasad Talluri V. S. S. L.

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tom 09

EN

In recent years, there has been a phenomenal increase in the use of alkaline proteases as industrial catalysts. The aim of this work was to isolate potent fungal strain from the agricultural field of Gulbarga region of India, for the production of alkaline protease by utilizing the agricultural by products viz, red and green gram and Bengal gram as substrate under submerged fermentation process. Optimization of fermentation process parameters such as substrate (Red gram husk, green gram husk and Bengal gram husk) utilization, utilization, temperature, pH and incubation period for alkaline protease production was carried out. The maximum production of alkaline protease by Trichoderma VPG 12 was found at pH 8, temperature 35 °C, incubated for 120 h. But the activity of the enzyme could also be seen in a wide range of pH (5-9) and temperature (20-40 °C). With all these properties, the strain can be considered for industrial grade production of alkaline protease.