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A Novel Cold-Adapted and High-Alkaline Alginate Lyase with Potential for Alginate Oligosaccharides Preparation

文献类型： 外文期刊

作者： Wang, Hai-Ying 1 ; Chen, Zhi-Fang 1 ; Zheng, Zhi-Hong 1 ; Lei, Hui-Wen 1 ; Cong, Hai-Hua 5 ; Zhou, Hai-Xiang 2 ;

作者机构： 1.Chinese Acad Fishery Sci, Key Lab Sustainable Dev Polar Fishery, Minist Agr & Rural Affairs, Yellow Sea Fisheries Res Inst, Qingdao 266071, Peoples R China

2.Shandong Peanut Res Inst, Qingdao 266100, Peoples R China

3.Dalian Ocean Univ, Coll Fisheries & Life Sci, Dalian 116023, Peoples R China

4.Dalian Ocean Univ, Coll Food Sci & Engn, Dalian 116023, Peoples R China

5.Suzhou Polytech Inst Agr, Coll Food Sci & Technol, Suzhou 215008, Peoples R China

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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