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

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 unde...

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Bibliographic Details
Published in:Archives of microbiology 2001-12, Vol.177 (1), p.91-97
Main Authors: Adham, S.A.I, Honrubia, P, Diaz, M, Fernandez-Abalos, J.M, Santamaria, R.I, Gil, J.A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins
Bacteriology
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
Brevibacterium - enzymology
Brevibacterium - genetics
Brevibacterium lactofermentum
celA1 gene
cellulase
Cellulase - genetics
Cellulase - metabolism
Cellulose 1,4-beta-Cellobiosidase
Cloning, Molecular
Corynebacterium glutamicum
Culture Media
endo-1,4-beta-glucanase
enzyme activity
Escherichia coli
Fundamental and applied biological sciences. Psychology
gene expression
genes
genetic vectors
Genetics
hosts
kanamycin
Microbiology
Mission oriented research
Molecular Sequence Data
Plasmids
signal peptide
Streptomyces - enzymology
Streptomyces - genetics
Streptomyces - metabolism
Streptomyces halstedii
xylanases
Xylosidases - genetics
Xylosidases - metabolism
xysA gene
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Summary: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.
ISSN:0302-8933
1432-072X
DOI:10.1007/s00203-001-0365-3