Abstract
Clostridium acetobutylicum mutants BA 101 (hyperamylolytic) and BA 105 (catabolite depressed) were isolated by using N-methyl-N'-nitro-N-nitrosoguanidine together with selective enrichment on the glucose analog 2-deoxyglucose. Amylolytic enzyme production by C. acetobutylicum BA 101 was 1.8- and 2.5-fold higher than that of the ATCC 824 strain grown in starch and glucose, respectively. C. acetobutylicum BA 105 produced 6.5-fold more amylolytic activity on glucose relative to that of the wild-type strain. The addition of glucose at time zero to starch-based P2 medium reduced the total amylolytic activities of C. acetobutylicum BA 101 and BA 105 by 82 and 25%, respectively, as compared with the activities of the same strains grown on starch alone. Localization studies demonstrated that the amylolytic activities of C. acetobutylicum BA 101 and BA 105 were primarily extracellular on all carbohydrates tested.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Annous B. A., Blaschek H. P. Regulation and localization of amylolytic enzymes in Clostridium acetobutylicum ATCC 824. Appl Environ Microbiol. 1990 Aug;56(8):2559–2561. doi: 10.1128/aem.56.8.2559-2561.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Botsford J. L. Cyclic nucleotides in procaryotes. Microbiol Rev. 1981 Dec;45(4):620–642. doi: 10.1128/mr.45.4.620-642.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bowring S. N., Morris J. G. Mutagenesis of Clostridium acetobutylicum. J Appl Bacteriol. 1985 Jun;58(6):577–584. doi: 10.1111/j.1365-2672.1985.tb01714.x. [DOI] [PubMed] [Google Scholar]
- Clementi F., Rossi J., Costamagna L., Rosi J. Production of amylase(s) by Schwanniomyces castellii and Endomycopsis fibuligera. Antonie Van Leeuwenhoek. 1980;46(4):399–405. doi: 10.1007/BF00421986. [DOI] [PubMed] [Google Scholar]
- Hockenhull D. J., Herbert D. The amylase and maltase of Clostridium acetobutylicum. Biochem J. 1945;39(1):102–106. doi: 10.1042/bj0390102. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hyun H. H., Zeikus J. G. Regulation and genetic enhancement of beta-amylase production in Clostridium thermosulfurogenes. J Bacteriol. 1985 Dec;164(3):1162–1170. doi: 10.1128/jb.164.3.1162-1170.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ingle M. B., Erickson R. J. Bacterial alpha-amylases. Adv Appl Microbiol. 1978;24:257–278. [PubMed] [Google Scholar]
- Lin Y. L., Blaschek H. P. Butanol Production by a Butanol-Tolerant Strain of Clostridium acetobutylicum in Extruded Corn Broth. Appl Environ Microbiol. 1983 Mar;45(3):966–973. doi: 10.1128/aem.45.3.966-973.1983. [DOI] [PMC free article] [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]
- Priest F. G. Extracellular enzyme synthesis in the genus Bacillus. Bacteriol Rev. 1977 Sep;41(3):711–753. doi: 10.1128/br.41.3.711-753.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Saier M. H., Jr Protein phosphorylation and allosteric control of inducer exclusion and catabolite repression by the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Microbiol Rev. 1989 Mar;53(1):109–120. doi: 10.1128/mr.53.1.109-120.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weickert M. J., Chambliss G. H. Site-directed mutagenesis of a catabolite repression operator sequence in Bacillus subtilis. Proc Natl Acad Sci U S A. 1990 Aug;87(16):6238–6242. doi: 10.1073/pnas.87.16.6238. [DOI] [PMC free article] [PubMed] [Google Scholar]