- Molecular characterization of SCO0765 as a cellotriose releasing endo-β-1,4-cellulase from Streptomyces coelicolor A(3)
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Joo-Bin Hong , Vijayalakshmi Dhakshnamoorthy , Chang-Ro Lee
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J. Microbiol. 2016;54(9):626-631. Published online August 31, 2016
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DOI: https://doi.org/10.1007/s12275-016-6271-9
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The sco0765 gene was annotated as a glycosyl hydrolase family
5 endoglucanase from the genomic sequence of Streptomyces
coelicolor A3(2) and consisted of 2,241 bp encoding a
polypeptide of 747 amino acids (molecular weight of 80.5
kDa) with a 29-amino acid signal peptide for secretion. The
SCO0765 recombinant protein was heterogeneously overexpressed
in Streptomyces lividans TK24 under the control
of a strong ermE* promoter. The purified SCO0765 protein
showed the expected molecular weight of the mature form
(718 aa, 77.6 kDa) on sodium dodecyl sulfate-polyacryl amide
gel electrophoresis. SCO0765 showed high activity toward
β-glucan and carboxymethyl cellulose (CMC) and negligible
activity to Avicel, xylan, and xyloglucan. The SCO0765 cellulase
had a maximum activity at pH 6.0 and 40°C toward
CMC and at pH 9.0 and 50–60°C toward β-glucan. Thin
layer chromatography of the hydrolyzed products of CMC
and β-glucan by SCO0765 gave cellotriose as the major product
and cellotetraose, cellopentaose, and longer oligosaccharides
as the minor products. These results clearly demonstrate
that SCO0765 is an endo-β-1,4-cellulase, hydrolyzing
the β-1,4 glycosidic bond of cellulose into cellotriose.
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Citations
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International Journal of Molecular Sciences.2024; 25(2): 1051. CrossRef - Haloferax sulfurifontis GUMFAZ2 producing xylanase‐free cellulase retrieved from Haliclona sp. inhabiting rocky shore of Anjuna, Goa‐India
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Applied Microbiology and Biotechnology.2019; 103(20): 8403. CrossRef
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