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KMID : 0545119990090040443
Journal of Microbiology and Biotechnology
1999 Volume.9 No. 4 p.443 ~ p.449
Production of a Fihrinolytic Enzyme in Bioreactor Culture by BaciIIus subtilis BK-17
Lee, Jin Wook
Park, Sung Yurb/Choi, Won A/Lee, Kyung Hee/Jeong, Yong Kee/Kong, In Soo/Park, Sung Hoon
Abstract
Bacillus subtilis BK-17 which produces a novel protease with fibrinolytic activity was isolated from soybean paste. Bioreactor production of the enzyme was studied in order to optimize fermentation conditions such as medium concentration, pH, agitation speed, and temperature. Under most cultural conditions, enzyme production initially began when the cell growth stopped. The onset of the enzyme production was indicated by rapid increase in both dissolved oxygen (DO) and pH. Two- to three-times more concentrated medium than the flask optimum medium yielded higher enzyme production in the bioreactor fermentation, When the medium pH was controlled constant, pH 6.5 exhibited the highest activity in the range of 6.0 to 7.5, but the activity was similar to the case when the pH was initially adjusted to 7.5 and subsequently maintained within a relatively wide range of 6.4 to 7.8. Agitation speed did not affect the enzyme production with an exception of DO reaching zero. Fermentation time was reduced when temperature increased within the range of 25¡É to 37¡É. However, the highest activity, along with the slow decrease of the enzymatic activity after reaching the maximum value, was observed at 25¡É. By shifting the temperature from 37¡É to 25¡É immediately after DO reached the minimum level, the high enzyme production of 1,100 U/§¢ along with the short fermentation period of 13 h could be obtained.
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