Abstract
The production of α-amylase, pullulanase, and α-glucosidase and the formation of fermentation products by the newly isolated thermophilic Clostridium sp. strain EM1 were investigated in continuous culture with a defined medium and an incubation temperature of 60°C. Enzyme production and excretion were greatly influenced by the dilution rate and the pH of the medium. The optimal values for the formation of starch-hydrolyzing enzymes were a pH of 5.9 and a dilution rate of 0.075 to 0.10 per h. Increase of the dilution rate from 0.1 to 0.3 per h caused a drastic drop in enzyme production. The ethanol concentration and optical density of the culture, however, remained almost constant. Growth limitation in the chemostat with 1% (wt/vol) starch was found optimal for enzyme production. Under these conditions 2,800 U of pullulanase per liter and 1,450 U of α-amylase per liter were produced; the amounts excreted were 70 and 55%, respectively.
Full text
PDFSelected References
These references are in PubMed. This may not be the complete list of references from this article.
- Friedrich C. G. Depression of hydrogenase during limitation of electron donors and derepression of ribulosebisphosphate carboxylase during carbon limitation of Alcaligenes eutrophus. J Bacteriol. 1982 Jan;149(1):203–210. doi: 10.1128/jb.149.1.203-210.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hyun H. H., Zeikus J. G. General Biochemical Characterization of Thermostable Pullulanase and Glucoamylase from Clostridium thermohydrosulfuricum. Appl Environ Microbiol. 1985 May;49(5):1168–1173. doi: 10.1128/aem.49.5.1168-1173.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hyun H. H., Zeikus J. G. Simultaneous and Enhanced Production of Thermostable Amylases and Ethanol from Starch by Cocultures of Clostridium thermosulfurogenes and Clostridium thermohydrosulfuricum. Appl Environ Microbiol. 1985 May;49(5):1174–1181. doi: 10.1128/aem.49.5.1174-1181.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Madi E., Antranikian G., Ohmiya K., Gottschalk G. Thermostable amylolytic enzymes from a new clostridium isolate. Appl Environ Microbiol. 1987 Jul;53(7):1661–1667. doi: 10.1128/aem.53.7.1661-1667.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wolin E. A., Wolfe R. S., Wolin M. J. Viologen dye inhibition of methane formation by Methanobacillus omelianskii. J Bacteriol. 1964 May;87(5):993–998. doi: 10.1128/jb.87.5.993-998.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]