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从海洋细菌弗氏弧菌 H1 中鉴定一种新型海藻酸盐裂解酶。

Characterization of a Novel Alginate Lyase from Marine Bacterium Vibrio furnissii H1.

机构信息

Jiangsu Provincial Engineering Laboratory for Biomass Conversion and Process Integration, Huaiyin Institute of Technology, Huaian 223003, China.

School of Life Science and Food Engineering, Huaiyin Institute of Technology, Huaian 223003, China.

出版信息

Mar Drugs. 2018 Jan 15;16(1):30. doi: 10.3390/md16010030.

DOI:10.3390/md16010030
PMID:29342949
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5793078/
Abstract

Alginate lyases show great potential for industrial and medicinal applications, especially as an attractive biocatalyst for the production of oligosaccharides with special bioactivities. A novel alginate lyase, AlyH1, from the marine bacterium H1, which has been newly isolated from rotten seaweed, was purified and characterized. The purified enzyme showed the specific activity of 2.40 U/mg. Its molecular mass was 35.8 kDa. The optimal temperature and pH were 40 °C and pH 7.5, respectively. AlyH1 maintained stability at neutral pH (7.0-8.0) and temperatures below 30 °C. Metal ions Na⁺, Mg, and K⁺ increased the activity of the enzyme. With sodium alginate as the substrate, the m and max values of AlyH1 were 2.28 mg/mL and 2.81 U/mg, respectively. AlyH1 exhibited activities towards both polyguluronate and polymannuronate, and preferentially degraded polyguluronate. Products prepared from sodium alginate by AlyH1 were displayed to be di-, tri-, and tetra-alginate oligosaccharides. A partial amino acid sequence (190 aa) of AlyH1 analysis suggested that AlyH1 was an alginate lyase of polysaccharide lyase family 7. The sequence showed less than 77% identity to the reported alginate lyases. These data demonstrated that AlyH1 could be as a novel and potential candidate in application of alginate oligosaccharides production with low polymerization degrees.

摘要

海藻酸盐裂解酶在工业和医学应用方面具有巨大的潜力,特别是作为一种有吸引力的生物催化剂,可用于生产具有特殊生物活性的低聚糖。一种新型的海藻酸盐裂解酶 AlyH1 来自海洋细菌 H1,该细菌是从腐烂的海藻中分离出来的。该酶已被分离和纯化,并对其性质进行了研究。该酶的比活为 2.40 U/mg,分子量为 35.8 kDa。最适温度和 pH 分别为 40°C 和 pH7.5。AlyH1 在中性 pH(7.0-8.0)和低于 30°C 的温度下保持稳定。金属离子 Na⁺、Mg²⁺和 K⁺能提高酶的活性。以海藻酸钠为底物时,AlyH1 的 m 和 max 值分别为 2.28 mg/mL 和 2.81 U/mg。AlyH1 对聚古罗糖醛酸和聚甘露糖醛酸均有活性,且优先降解聚古罗糖醛酸。AlyH1 作用于海藻酸钠的产物为二、三、四聚海藻糖低聚糖。AlyH1 的部分氨基酸序列(190 aa)分析表明,AlyH1 属于多糖裂解酶家族 7 的海藻酸盐裂解酶。该序列与报道的海藻酸盐裂解酶的同源性小于 77%。这些数据表明 AlyH1 可能是一种新型的、有潜力的候选酶,可用于生产低聚合度的海藻酸盐低聚糖。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/548f/5793078/48dad772507d/marinedrugs-16-00030-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/548f/5793078/db1c47562021/marinedrugs-16-00030-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/548f/5793078/2f5311b1d590/marinedrugs-16-00030-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/548f/5793078/56951e38f64c/marinedrugs-16-00030-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/548f/5793078/48dad772507d/marinedrugs-16-00030-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/548f/5793078/db1c47562021/marinedrugs-16-00030-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/548f/5793078/2f5311b1d590/marinedrugs-16-00030-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/548f/5793078/56951e38f64c/marinedrugs-16-00030-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/548f/5793078/48dad772507d/marinedrugs-16-00030-g004.jpg

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