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Information Journal Paper

Title

ENZYME PRODUCTION OF BACILLUS IN SUBMERGED CULTURE

Pages

  23-27

Abstract

 Aim and Background: Proteases is family of ENZYMEs which has valuable commercial applications due to their very crucial physiological roles. Alkaline proteases is produced by Bacillus species which are of particular importance because of their thermal stability at different pHs. This study aimed to evaluate and compare two methods of package cultivation and semiconductor in immersed culture medium for the production of alkaline protease ENZYME using 2, 10 and 20 percent of glucose substrate.Materials and methods: Bacteria of the genus Bacillus were isolated from alkaline soils of Guilan province and after screening for ENZYME production being simultaneously evaluated in both. closed and semi-continuous culture methods.Results: Comparison of two methods showed that ENZYME production in semi-continuous culture was 2.3 times more than package culture using 2% glucose (0.207U / ml vs. 0.088 U / ml) indicating that the former is more effective.Conclusion: isolated Bacillus strains could produce alkaline protease ENZYME in both culture methods, but ENZYME activity in semi-continuous culture was 3.2 times higher compared to packageculture.

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  • Cite

    APA: Copy

    TEBYANIAN, HAMID, OTROSHI, BEHZAD, KARAMI, ALI, & BABAVALIAN, HAMID. (2016). ENZYME PRODUCTION OF BACILLUS IN SUBMERGED CULTURE. NEW CELLULAR & MOLECULAR BIOTECHNOLOGY JOURNAL, 6(22), 23-27. SID. https://sid.ir/paper/204622/en

    Vancouver: Copy

    TEBYANIAN HAMID, OTROSHI BEHZAD, KARAMI ALI, BABAVALIAN HAMID. ENZYME PRODUCTION OF BACILLUS IN SUBMERGED CULTURE. NEW CELLULAR & MOLECULAR BIOTECHNOLOGY JOURNAL[Internet]. 2016;6(22):23-27. Available from: https://sid.ir/paper/204622/en

    IEEE: Copy

    HAMID TEBYANIAN, BEHZAD OTROSHI, ALI KARAMI, and HAMID BABAVALIAN, “ENZYME PRODUCTION OF BACILLUS IN SUBMERGED CULTURE,” NEW CELLULAR & MOLECULAR BIOTECHNOLOGY JOURNAL, vol. 6, no. 22, pp. 23–27, 2016, [Online]. Available: https://sid.ir/paper/204622/en

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