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Proteases production from fermentation of fish solubles Lakhdari, Marc
Abstract
The possibility of using a culture medium derived from herring fish solubles to produce proteases was investigated. Following Wah-On's (27) recommandations, the role of the oxygen in the cell and enzyme production was specially considered. A Myxobacteria, Sorangium 495 was used to produce the protease. It was first confirmed that the organism was aerobic, and that glucose had a significant effect on growth and protease formation, according to experiments performed in 250 ml Erlenmeyer flasks and in a 7-liter fermentor. Two different sets of experiments were made in the latter fermentor, one using culture medium of initial protein content of about 4 mg (BSA)/ml, and another between 11 and 16 mg (BSA)/ml. The maximum enzyme activity of 2.47 unit/10 cc was noticed at DO = 100% saturation at the low initial protein content. It was then concluded that oxygen favors protease formation. However, although the importance of oxygen cannot be denied, no consistent pattern to the level of cell mass concentration as a function DO level could be found, and this role could not be accurately determined. Furthermore, the kinetic patterns were quite complex, and no simple correlation between the different parameters involved could be determined.
Item Metadata
Title |
Proteases production from fermentation of fish solubles
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Creator | |
Publisher |
University of British Columbia
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Date Issued |
1978
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Description |
The possibility of using a culture medium derived from herring fish solubles to produce proteases was investigated. Following Wah-On's (27) recommandations, the role of the oxygen in the cell and enzyme production was specially considered. A Myxobacteria, Sorangium 495 was used to produce the protease. It was first confirmed that the organism was aerobic, and that glucose had a significant effect on growth and protease formation, according to experiments performed in 250 ml Erlenmeyer flasks and in a 7-liter fermentor. Two different sets of experiments were made in the latter fermentor, one using culture medium of initial protein content of about 4 mg (BSA)/ml, and another between 11 and 16 mg (BSA)/ml. The maximum enzyme activity of 2.47 unit/10 cc was noticed at DO = 100% saturation at the low initial protein content. It was then concluded that oxygen favors protease formation. However, although the importance of oxygen cannot be denied, no consistent pattern to the level of cell mass concentration as a function DO level could be found, and this role could not be accurately determined. Furthermore, the kinetic patterns were quite complex, and no simple correlation between the different parameters involved could be determined.
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Type | |
Language |
eng
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Date Available |
2010-02-26
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Provider |
Vancouver : University of British Columbia Library
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Rights |
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.
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DOI |
10.14288/1.0058930
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URI | |
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Affiliation | |
Degree Grantor |
University of British Columbia
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Campus | |
Scholarly Level |
Graduate
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Aggregated Source Repository |
DSpace
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Rights
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.