Streptomyces lividans and Brevibacterium lactofermentum as heterologous hosts for the production of X22 xylanase from Aspergillus nidulans.
The Aspergillus nidulans gene xlnA coding for the fungal xylanase X22 has been cloned and expressed in two heterologous bacterial hosts: Streptomyces lividans and Brevibacterium lactofermentum. Streptomyces strains yielded 10 units/ml of xylanase when the protein was produced with its own signal peptide, and 19 units/ml when its signal peptide was replaced by the one for xylanase Xys1 from Streptomyces halstedii. B. lactofermentum was also able to produce xylanase X22, affording 6 units/ml upon using either the Aspergillus xlnA signal peptide or Streptomyces xysA. These production values are higher than those previously reported for the heterologous expression of the A. nidulans xlnA gene in Saccharomyces cerevisiae (1 unit/ml). Moreover, the X22 enzyme produced by Streptomyces lividans showed oenological properties, indicating that this Streptomyces recombinant strain is a good candidate for the production of this enzyme at the industrial scale.
Díaz
M
M
Instituto de Microbiología Bioquímica/Departamento de Microbiología y Genética, Consejo Superior de Investigaciones Científicas/Universidad de Salamanca, Edificio Departamental, Campus Miguel de Unamuno, 37007, Salamanca, Spain.
Adham
S A I
SA
Ramón
D
D
Gil
J A
JA
Santamaría
R I
RI
D001233:Aspergillus nidulans / Q000201:enzymology*; D001709:Biotechnology / Q000379:methods; D001951:Brevibacterium / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D015870:Gene Expression; D021382:Protein Sorting Signals / Q000235:genetics / Q000502:physiology; D011994:Recombinant Proteins / Q000032:analysis / Q000235:genetics / Q000302:isolation & purification; D013302:Streptomyces / Q000235:genetics / Q000378:metabolism*; D014995:Xylosidases / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification
D021382:Protein Sorting Signals; D011994:Recombinant Proteins; D014995:Xylosidases; C412196:xylanase X22