Oxygen transfer effects in serine alkaline protease fermentation by Bacillus licheniformis: Use of citric acid as the carbon source

Date

1998-12-01

Author

Çalık, Pınar

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The effects of oxygen transfer on serine alkaline protease (SAP) production by Bacillus licheniformis on a defined medium with C-c = 9.0 kg m(-3) citric acid as sole carbon source were investigated in 3.5 dm(3) batch bioreactor systems. The concentrations of the product (SAP) and by-products, i.e., neutral protease, amylase, amino acids, and organic acids were determined in addition to SAP activities. Ar Q(o)/V = 1 vvm airflow rate, the effect of agitation rate on DO concentration, pH, product, and by-product concentrations and SAP activity were investigated at N = 150, 500, and 750 min(-1); these are named as low-(LOT), medium-(MOT), and high oxygen transfer (HOT) conditions. LOT conditions favor biomass concentration; however, substrate consumption was highest at HOT conditions. MOT was optimum for maximum SAP activity which was 441 U cm(-3) at t = 37 h. The total amino acid concentration was maximum in LOT and minimum in MOT conditions; lysine had the highest concentration under all oxygen transfer conditions. Among organic acids, acetic acid had the highest concentration and its concentration increased with oxygen transfer rate. The oxygen transfer coefficient increases with the agitation rate and the oxygen consumption rate increased almost linearly with the biomass concentration. (C) 1998 Elsevier Science Inc.

Subject Keywords

Biotechnology, Applied Microbiology and Biotechnology, Biochemistry

URI

https://hdl.handle.net/11511/53144

Journal

ENZYME AND MICROBIAL TECHNOLOGY

DOI

https://doi.org/10.1016/s0141-0229(98)00069-6

Collections

Department of Chemical Engineering, Article

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Citation Formats

P. Çalık, “Oxygen transfer effects in serine alkaline protease fermentation by Bacillus licheniformis: Use of citric acid as the carbon source,” ENZYME AND MICROBIAL TECHNOLOGY, pp. 451–461, 1998, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/53144.