Please use this identifier to cite or link to this item: http://archive.cmb.ac.lk:8080/xmlui/handle/70130/5305
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dc.contributor.authorLee, Y-
dc.contributor.authorLee, J. H-
dc.contributor.authorShim, W. B-
dc.contributor.authorElvitigala, D. A. S.,-
dc.contributor.authorDe Zoysa, M-
dc.contributor.authorLee, S. J-
dc.contributor.authorKang, H.D-
dc.contributor.authorOh, C-
dc.date.accessioned2021-06-05T16:37:59Z-
dc.date.available2021-06-05T16:37:59Z-
dc.date.issued2014-
dc.identifier.citationLee, 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.en_US
dc.identifier.urihttp://archive.cmb.ac.lk:8080/xmlui/handle/70130/5305-
dc.description.abstractGlucanases 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 industriesen_US
dc.language.isoenen_US
dc.subjectβ-1,3-glucanaseen_US
dc.subjectMesoflavibacter zeaxanthinifaciensen_US
dc.subjectrecombinant enzymeen_US
dc.subjectlaminarinase activityen_US
dc.subjectbiochemical propertiesen_US
dc.titleMolecular Cloning, Over-expression and Enzymatic Characterization of an Endo-acting β-1,3-glucanase from Marine Bacterium Mesoflavibacter zeaxanthinifaciens S86 in Escherichia colien_US
dc.typeArticleen_US
Appears in Collections:Department of Basic Sciences & Social Sciences

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