Mutants of Erwinia chrysanthemi defective in secretion of pectinase and cellulase.
AUTOR(ES)
Andro, T
RESUMO
Erwinia chrysanthemi produced several pectate lyases (EC 4.2.2.2) and endocellulases (EC 3.2.1.4) which were largely secreted into the culture medium. Mutants deficient in the secretion mechanism for these enzymes were obtained by chemical and insertion mutagenesis. Further study of one such mutant revealed that both enzyme activities were retained simultaneously within the periplasmic space.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=215846Documentos Relacionados
- Molecular cloning of Erwinia chrysanthemi pectinase and cellulase structural genes
- Isolation and characterization of Erwinia chrysanthemi mutants defective in degradation of hexuronates.
- Characterization and virulence properties of Erwinia chrysanthemi lipopolysaccharide-defective, phi EC2-resistant mutants.
- The Erwinia chrysanthemi pecT gene regulates pectinase gene expression.
- In vivo cloning of the pectate lyase and cellulase genes of Erwinia chrysanthemi