期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 120, 期 -, 页码 729-735出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2018.08.164
关键词
Alginate lyase; Oligosaccharide; Cold-adaption; Metal ions resistance
资金
- Natural Science Foundation of Shandong Province [ZR2018MD021, ZR2015CM024]
- National Key Technology R&D Program of the Ministry of Science and Technology [2013BAB01B02]
- National High-Tech R&D Program of China [2014AA093504]
Alginate lyase played an important role in brown algae degradation, and its enzymatic degradation products showed various biological activities. Although many alginate lyases have been characterized, the enzymes with special characterizations are still rather rare. In this study, a new alginate lyase gene, tsaly6A, has been cloned from marine bacterium Thalassomonas sp. LD5, and expressed in Escherichia coli, The deduced alginate lyase, TsAly6A, belonged to the polysaccharide lyase (PL) family 6 and showed the highest amino acid identity (63%) with an exo-type oligoalginate lyase AIyGC. However, this study showed that TsAly6A was an endo-type enzyme yielding alginate trisaccharides (64.5%) as the main products. Compared with other alginate lyases, TsAly6A showed high trisaccharide-yielding levels. Meanwhile, TsAly6A showed the specific activity of 15,960 U/mu mol at its optimal pH (pH 8.0) and temperature (35 degrees C). In addition, TsAly6A was a cold-adapted, salt-activated and metal ions-resisted alginate lyase, which will enable it to perform high activity in the solution containing various ions. Its cold-adaptation, metal ions-tolerance and high trisaccharides yields make TsAly6A an excellent candidate for industrial applications. (C) 2018 Elsevier B.V. All rights reserved.
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