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http://archive.cmb.ac.lk:8080/xmlui/handle/70130/5305
Title: | Molecular Cloning, Over-expression and Enzymatic Characterization of an Endo-acting β-1,3-glucanase from Marine Bacterium Mesoflavibacter zeaxanthinifaciens S86 in Escherichia coli |
Authors: | Lee, Y Lee, J. H Shim, W. B Elvitigala, D. A. S., De Zoysa, M Lee, S. J Kang, H.D Oh, C |
Keywords: | β-1,3-glucanase Mesoflavibacter zeaxanthinifaciens recombinant enzyme laminarinase activity biochemical properties |
Issue Date: | 2014 |
Citation: | Lee, Y., Lee, J. H., Shim, W. B., Elvitigala, D. A. S., De Zoysa, M., Lee, S. J., ... & Oh, C. (2014). Molecular cloning, over-expression and enzymatic characterization of an endo-acting β-1, 3-glucanase from marine bacterium Mesoflavibacter zeaxanthinifaciens S86 in Escherichia coli. Ocean Science Journal, 49(4), 425-432. |
Abstract: | Glucanases are involved in degradation of glucans. Here, we report a new endo-β-1,3-glucanase Mzl86 identified in Mesoflavibacter zeaxanthinifaciens S86. The deduced amino-acid sequence of Mzl86 showed highest similarity (45.1%) with Leeuwenhoekiella blandensi and thus placed in glycosyl hydrolase family 16. Purified recombinant protein (rMz186) showed an optimum enzyme activity against laminarin at 50°C and pH 8. The enzyme was stable at 50°C for 1 hour (maintaining 80% of its maximum activity) and was strongly activated (187%) in the presence of 2.5 mM manganese. Substrate-specific activities of rMzl86 against laminarin, barley β-glucan and lichenan were 261, 128 and 115 unit/mg, respectively. rMzl86 degraded laminarioligosaccharides (lager than biose) and laminarin while producing mainly biose and glucose. Molecular and biochemical properties reveal that rMzl86 shares typical features of β-1,3-glucanase (EC 3.2.1.39) and thus is a potential candidate for use in agriculture, drug, chemical and bioethanol industries |
URI: | http://archive.cmb.ac.lk:8080/xmlui/handle/70130/5305 |
Appears in Collections: | Department of Basic Sciences & Social Sciences |
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