Cloning, Secretory Expression and Characterization of a Unique pH-Stable and Cold-Adapted Alginate Lyase
文献类型： 外文期刊
作者： Wang, Zhi-Peng 1 ; Cao, Min 2 ; Li, Bing 2 ; Ji, Xiao-Feng 1 ; Zhang, Xin-Yue 2 ; Zhang, Yue-Qi 2 ; Wang, Hai-Ying 1 ;
作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Key Lab Sustainable Dev Polar Fishery, Minist Agr & Rural Affairs, Qingdao 266071, Peoples R China
2.Qingdao Agr Univ, Marine Sci & Engn Coll, Qingdao 266109, Peoples R China
3.Yellow Sea Fisheries Res Inst, Lab Enzyme Engn, Qingdao 266071, Peoples R China
4.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Drugs & Bioprod, Qingdao 266071, Peoples R China
关键词： alginate lyase; cold-adapted; pH-stable; NaCl-independent
期刊名称：MARINE DRUGS （ 影响因子：5.118； 五年影响因子：5.951 ）
ISSN：
年卷期： 2020 年 18 卷 4 期
页码：
收录情况： SCI
摘要： Cold-adapted alginate lyases have unique advantages for alginate oligosaccharide (AOS) preparation and brown seaweed processing. Robust and cold-adapted alginate lyases are urgently needed for industrial applications. In this study, a cold-adapted alginate lyase-producing strain Vibrio sp. W2 was screened. Then, the gene ALYW201 was cloned from Vibrio sp. W2 and expressed in a food-grade host, Yarrowia lipolytica. The secreted Alyw201 showed the activity of 64.2 U/mL, with a molecular weight of approximate 38.0 kDa, and a specific activity of 876.4 U/mg. Alyw201 performed the highest activity at 30 degrees C, and more than 80% activity at 25-40 degrees C. Furthermore, more than 70% of the activity was obtained in a broad pH range of 5.0-10.0. Alyw201 was also NaCl-independent and salt-tolerant. The degraded product was that of the oligosaccharides of DP (Degree of polymerization) 2-6. Due to its robustness and its unique pH-stable property, Alyw201 can be an efficient tool for industrial production.
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