期刊
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
卷 126, 期 2, 页码 169-175出版社
SOC BIOSCIENCE BIOENGINEERING JAPAN
DOI: 10.1016/j.jbiosc.2018.02.018
关键词
Pseudoalteromonas; Laminarinase; Cold-adapted; Laminarioligosaccharide; Domain structure
资金
- Japan Society for the Promotion of Science KAKENHI [24580299]
- Grants-in-Aid for Scientific Research [24580299] Funding Source: KAKEN
We isolated a laminarin-degrading cold-adapted bacterium strain LA from coastal seawater in Sagami Bay, Japan and identified it as a Pseudoalteromonas species. We named the extracellular laminarinase LA-Lam, and purified and characterized it. LA-Lam showed high degradation activity for Laminaria digitata laminarin in the ranges of 15-50 degrees C and pH 5.0-9.0. The major terminal products degraded from L digitata laminarin with LA-Lam were glucose, laminaribiose, and laminaritriose. The degradation profile of laminarioligosaccharides with LA-Lam suggested that the enzyme has a high substrate binding ability toward tetrameric or larger saccharides. Our results of the gene sequence and the SDS-PAGE analyses revealed that the major part of mature LA-Lam is a catalytic domain that belongs to the GH16 family, although its precursor is composed of a signal peptide, the catalytic domain, and three-repeated unknown regions. (C) 2018, The Society for Biotechnology, Japan. All rights reserved.
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