Expression of the genes coding for the xylanase Xys1 and the cellulase Cel1 from the straw-decomposing Streptomyces halstedii JM8 cloned into the amino-acid producer Brevibacterium lactofermentum ATCC13869

Sirin A. Adham, Pilar Honrubia, Margarita Díaz, José M. Fernández-Abalos, Ramón I. Santamaría, José A. Gil

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

The xylanase (xysA) and the cellulase (celA1) genes from Streptomyces halstedii JM8 were cloned into Escherichia coli/Brevibacterium lactofermentum shuttle vectors and successfully expressed in both hosts when placed downstream from the kanamycin resistance promoter (Pkan) from Tn5 but not when under the control of their own promoters. Xylanase was secreted into the culture media of B. lactofermentum by removal of the same leader peptide as is removed in S. halstedii. The main difference between the production of xylanase by Streptomyces and corynebacteria was the low level of processing of the mature extracellular xylanase by B. lactofermentum, probably due to the lack of protease activity in this microorganism.

Original languageEnglish
Pages (from-to)91-97
Number of pages7
JournalArchives of Microbiology
Volume177
Issue number1
DOIs
Publication statusPublished - 2002

Fingerprint

Brevibacterium
Endo-1,4-beta Xylanases
Genetic Vectors
Kanamycin
Cellulase
Straw
Streptomyces
Protein Sorting Signals
Microorganisms
Escherichia coli
Culture Media
Peptide Hydrolases
Genes
Kanamycin Resistance
Gene Expression
Amino Acids
Corynebacterium
Processing

Keywords

  • Cellulase
  • Corynebacteria
  • Leader peptide
  • Proteolytic processing
  • Secretion
  • Xylanase

ASJC Scopus subject areas

  • Microbiology

Cite this

Expression of the genes coding for the xylanase Xys1 and the cellulase Cel1 from the straw-decomposing Streptomyces halstedii JM8 cloned into the amino-acid producer Brevibacterium lactofermentum ATCC13869. / Adham, Sirin A.; Honrubia, Pilar; Díaz, Margarita; Fernández-Abalos, José M.; Santamaría, Ramón I.; Gil, José A.

In: Archives of Microbiology, Vol. 177, No. 1, 2002, p. 91-97.

Research output: Contribution to journalArticle

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