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1
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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
|
2018
|
tom 71
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.
2
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Alkaline trypsin from the viscera and heads of Engraulis anchoita: partial purification and characterization

84%
Lamas D. L., Yeannes M. I., Massa A. E.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
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2017
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tom 98
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nr 2
3

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.
Acta Biochimica Polonica
|
2011
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tom 58
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nr 4
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
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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.
International Letters of Natural Sciences
|
2014
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tom 09
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.
5

Optimization and purification of alkaline proteases produced by marine Bacillus sp. MIG newly isolated from Eastern Harbour of Alexandria

67%
Gouda M. K.
Polish Journal of Microbiology
|
2006
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tom 55
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nr 2
A marine Bacillus strain was isolated from the eastern harbour of Alexandria and identified as Bacillus sp. MIG. Maximum activity of studied proteases was obtained when the bacterium was grown in medium with 1 % wheat bran and 0.5% yeast extract in addition to the mineral salts and incubated for 48 h at 30°C and 120 rpm. Two alkaline proteases (Pro 1 and Pro 2) were purified to homogeneity using cation exchange chromatography on CM-Sepharose CL-6B followed by Sephadex G-75 superfine. The optimum activities were at pH 11 or 12, and temperatures of 50 and 55°C for Pro 1 and Pro 2 respectively. These two enzymes were relatively stable over pH range from 7.0-11. Pro 2 was found to be more stable at 50°C in absence of Ca²⁺ and retained about 47% of its activity after 3 h at this temperature, while Pro 1 lost its activity completely at the same conditions. The two enzymes were active against haemoglobin and casein; in addition, Pro 2 exhibited moderate activity against keratin. Both enzymes were partially inhibited by Ag⁺ and Hg²⁺. PMSF completely inhibited the enzymes, while dithiothreitol and 2-mercaptoethanol stimulated their activities, suggesting to be thiol-dependent serine proteases. The enzymes were stable in the presence of the surfactants and bleaching agent (H₂O₂) and relatively stable in presence of some commercial detergents.
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