A Novel Cold-Adapted and High-Alkaline Alginate Lyase with Potential for Alginate Oligosaccharides Preparation
文献类型: 外文期刊
第一作者: Wang, Hai-Ying
作者: Wang, Hai-Ying;Chen, Zhi-Fang;Zheng, Zhi-Hong;Lei, Hui-Wen;Chen, Zhi-Fang;Zhou, Hai-Xiang;Chen, Zhi-Fang;Zheng, Zhi-Hong;Lei, Hui-Wen;Cong, Hai-Hua
作者机构:
关键词: alginate lyase; cold-adapted; high-alkaline; alginate oligosaccharides; Yarrowia lipolytica
期刊名称:MOLECULES ( 影响因子:4.6; 五年影响因子:4.9 )
ISSN:
年卷期: 2023 年 28 卷 17 期
页码:
收录情况: SCI
摘要: Alginate oligosaccharides (AOs) prepared through enzymatic reaction by diverse alginate lyases under relatively controllable and moderate conditions possess versatile biological activities. But widely used commercial alginate lyases are still rather rare due to their poor properties (e.g., lower activity, worse thermostability, ion tolerance, etc.). In this work, the alginate lyase Alyw208, derived from Vibrio sp. W2, was expressed in Yarrowia lipolytica of food grade and characterized in order to obtain an enzyme with excellent properties adapted to industrial requirements. Alyw208 classified into the polysaccharide lyase (PL) 7 family showed maximum activity at 35 degrees C and pH 10.0, indicating its cold-adapted and high-alkaline properties. Furthermore, Alyw208 preserved over 70% of the relative activity within the range of 10-55 degrees C, with a broader temperature range for the activity compared to other alginate-degrading enzymes with cold adaptation. Recombinant Alyw208 was significantly activated with 1.5 M NaCl to around 2.1 times relative activity. In addition, the endolytic Alyw208 was polyG-preferred, but identified as a bifunctional alginate lyase that could degrade both polyM and polyG effectively, releasing AOs with degrees of polymerization (DPs) of 2-6 and alginate monomers as the final products (that is, DPs 1-6). Alyw208 has been suggested with favorable properties to be a potent candidate for biotechnological and industrial applications.
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