Isolation and characterization of Clostridium acetobutylicum mutants with enhanced amylolytic activity.
AUTOR(ES)
Annous, B A
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=183617Documentos Relacionados
- Isolation and characterization of butanol-resistant mutants of Clostridium acetobutylicum.
- Isolation and characterization of Bordetella bronchiseptica mutants deficient in siderophore activity.
- Regulation and localization of amylolytic enzymes in Clostridium acetobutylicum ATCC 824.
- Isolation and characterization of an extracellular glycosylated protein complex from Clostridium thermosaccharolyticum with pectin methylesterase and polygalacturonate hydrolase activity.
- Isolation and characterization of a filamentous viruslike particle from Clostridium acetobutylicum NCIB 6444.
