Comparative characterization of three bacterial exo-type alginate lyases

Alginate, a major acidic polysaccharide in brown macroalgae, has attracted attention as a carbon source for production of ethanol and other chemical compounds. Alginate is monomerized by exo-type alginate lyase into an unsaturated uronate; thus, this enzyme is critical for the saccharification and u...

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Bibliographic Details
Published in:International journal of biological macromolecules 2016-05, Vol.86, p.519-524
Main Authors: Hirayama, Makoto, Hashimoto, Wataru, Murata, Kousaku, Kawai, Shigeyuki
Format: Article
Language:English
Subjects:
Agrobacterium tumefaciens
Alginate
Bacteria
Bacteria - enzymology
Enzyme Stability
Exo-type alginate lyase
Polysaccharide-Lyases - chemistry
Polysaccharide-Lyases - isolation & purification
Polysaccharide-Lyases - metabolism
Sphingomonas
Uronate
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Summary:Alginate, a major acidic polysaccharide in brown macroalgae, has attracted attention as a carbon source for production of ethanol and other chemical compounds. Alginate is monomerized by exo-type alginate lyase into an unsaturated uronate; thus, this enzyme is critical for the saccharification and utilization of alginate. Although several exo-type alginate lyases have been characterized independently, their activities were not assayed under the same conditions or using the same unit definition, making it difficult to compare enzymatic properties or to select the most suitable enzyme for saccharification of alginate. In this study, we characterized the three bacterial exo-type alginate lyases under the same conditions: A1–IV of Sphingomonas sp. strain A1, Atu3025 of Agrobacterium tumefaciens, and Alg17c of Saccharophagus degradans. A1–IV had the highest specific activity as well as the highest productivity of uronate, whereas Alg17c had the lowest activity and productivity. Only dialyzed Atu3025 and Alg17c were tolerant to freezing. Alg17c exhibited a remarkable halotolerance, which may be advantageous for monomerization of alginate from marine brown algae. Thus, each enzyme exhibited particular desirable and undesirable properties. Our results should facilitate further utilization of the promising polysaccharide alginate.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2016.01.095