Large-scale production of a thermostable Rhodothermus marinus cellulase by heterologous secretion from Streptomyces lividans

Soliman, Mohamed Belal Hamed; Karamanou, Spyridoula; Ólafsdottir, Solveig; Basílio, Joana Sofia Martins; Simoens, Kenneth; Tsolis, Kostantinos C; Van Mellaert, Lieve; Guðmundsdóttir, Eik Elísabet; Hreggvidsson, Gudmundur Oli; Anné, Jozef; Bernaerts, Kristel; Fridjonsson, Olafur H; Economou, Anastassios

doi:10.1186/s12934-017-0847-x

Large-scale production of a thermostable Rhodothermus marinus cellulase by heterologous secretion from Streptomyces lividans

Author:

Soliman, Mohamed Belal Hamed

Karamanou, Spyridoula ; Ólafsdottir, Solveig ; Basílio, Joana Sofia Martins ; Simoens, Kenneth ; Tsolis, Kostantinos C ; Van Mellaert, Lieve ; Guðmundsdóttir, Eik Elísabet ; Hreggvidsson, Gudmundur Oli ; Anné, Jozef ; Bernaerts, Kristel ; Fridjonsson, Olafur H ; Economou, Anastassios

Keywords:

Science & Technology, Life Sciences & Biomedicine, Biotechnology & Applied Microbiology, Cellulase, Protein translocase, Signal peptide, Secretion, Streptomyces lividans, Protein secretion biotechnology, PROTEIN-PRODUCTION, MYCOBACTERIUM-TUBERCULOSIS, EXPRESSION, GENE, ENDOGLUCANASE, DYNAMICS, ALPHA, MOTOR, Bacterial Proteins, Enzyme Stability, Gene Expression, Hot Temperature, Protein Transport, Rhodothermus, 0605 Microbiology, 1003 Industrial Biotechnology, Biotechnology, 3107 Microbiology

Abstract:

The gene encoding a thermostable cellulase of family 12 was previously isolated from a Rhodothermus marinus through functional screening. CelA is a protein of 260 aminoacyl residues with a 28-residue amino-terminal signal peptide. Mature CelA was poorly synthesized in some Escherichia coli strains and not at all in others. Here we present an alternative approach for its heterologous production as a secreted polypeptide in Streptomyces.