Abstract
An alkaline-thermostable mannanase from Streptomyces sp. CS428 was produced, purified, and biochemically characterized. The extracellular mannanase (Mn428) was purified to homogeneity with 12.4 fold, specific activity of 2406.7 U/mg, and final recovery of 37.6 %. The purified β-mannanase was found to be a monomeric protein with a molecular mass of approximately 35 kDa as analyzed by SDS-PAGE and zymography. The first N-terminal amino acid sequences of mannanase enzyme were HIRNGNHQLPTG. The optimal temperature and pH for enzyme were 60 °C and 12.5, respectively. The mannanase activities were significantly affected by the presence of metal ions, modulators, and detergents. Km and Vmax values of Mn428 were 1.01 ± 3.4 mg/mL and 5029 ± 85 µmol/min mg, respectively when different concentrations (0.6–10 mg/mL) of locust bean gum galactomannan were used as substrate. The substrate specificity of enzyme showed its highest specificity towards galactomannan which was further hydrolyzed to produce mannose, mannobiose, mannotriose, and a series of mannooligosaccharides. Mannooligosaccharides can be further converted to ethanol production, thus the purified β-mannanase isolated from Streptomyces sp. CS428 was found to be attractive for biotechnological applications.
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This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korean government (MEST) (NRF-2015R1A2A1A15056120, NRF-2015R1D1A1A 010 59 483) and Bio-industry Technology Development Program, Ministry of Agriculture, Food and Rural Affairs (115073-2).
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Pradeep G. C. and Seung Sik Cho have contributed equally to this work.
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Pradeep G. C., Cho, S.S., Choi, Y.H. et al. An extremely alkaline mannanase from Streptomyces sp. CS428 hydrolyzes galactomannan producing series of mannooligosaccharides. World J Microbiol Biotechnol 32, 84 (2016). https://doi.org/10.1007/s11274-016-2040-5
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DOI: https://doi.org/10.1007/s11274-016-2040-5