Comparative characterization of three bacterial exo-type alginate lyases

被引:18
作者
Hirayama, Makoto [1 ]
Hashimoto, Wataru [1 ]
Murata, Kousaku [2 ]
Kawai, Shigeyuki [1 ]
机构
[1] Kyoto Univ, Grad Sch Agr, Div Food Sci & Biotechnol, Lab Basic & Appl Mol Biotechnol, Kyoto 6110011, Japan
[2] Setsunan Univ, Dept Life Sci, Fac Sci & Engn, Neyagawa, Osaka, Japan
关键词
Alginate; Exo-type alginate lyase; Uronate; SPHINGOMONAS SP A1; ESCHERICHIA-COLI; AGROBACTERIUM-TUMEFACIENS; MOLECULAR-IDENTIFICATION; COMPLEX POLYSACCHARIDES; OLIGOALGINATE LYASE; BROWN MACROALGAE; OVEREXPRESSION; PURIFICATION; ACID;
D O I
10.1016/j.ijbiomac.2016.01.095
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2016 Elsevier B.V. All rights reserved.
引用
收藏
页码:519 / 524
页数:6
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