Please use this identifier to cite or link to this item:
http://archive.cmb.ac.lk:8080/xmlui/handle/70130/5305
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Y | - |
dc.contributor.author | Lee, J. H | - |
dc.contributor.author | Shim, W. B | - |
dc.contributor.author | Elvitigala, D. A. S., | - |
dc.contributor.author | De Zoysa, M | - |
dc.contributor.author | Lee, S. J | - |
dc.contributor.author | Kang, H.D | - |
dc.contributor.author | Oh, C | - |
dc.date.accessioned | 2021-06-05T16:37:59Z | - |
dc.date.available | 2021-06-05T16:37:59Z | - |
dc.date.issued | 2014 | - |
dc.identifier.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. | en_US |
dc.identifier.uri | http://archive.cmb.ac.lk:8080/xmlui/handle/70130/5305 | - |
dc.description.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 | en_US |
dc.language.iso | en | en_US |
dc.subject | β-1,3-glucanase | en_US |
dc.subject | Mesoflavibacter zeaxanthinifaciens | en_US |
dc.subject | recombinant enzyme | en_US |
dc.subject | laminarinase activity | en_US |
dc.subject | biochemical properties | en_US |
dc.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 | en_US |
dc.type | Article | en_US |
Appears in Collections: | Department of Basic Sciences & Social Sciences |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.