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Secretory Expression of an Alkaline Alginate Lyase With Heat Recovery Property in Yarrowia lipolytica

文献类型： 外文期刊

作者： Liu, Lu 1 ; Wang, Zhipeng 3 ; Zheng, Zhihong 4 ; Li, Ze 5 ; Ji, Xiaofeng 1 ; Cong, Haihua 4 ; Wang, Haiying 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, Peoples R China

2.Ocean Univ China, Sch Med & Pharm, Qingdao, Peoples R China

3.Qingdao Agr Univ, Sch Marine Sci & Engn, Qingdao, Peoples R China

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

5.Linyi Vocat Univ Sci & Technol, Coll Adv Agr Sci, Linyi, Shandong, Peoples R China

关键词： alginate lyase; heat recovery; Yarrowia lipolytica; NaCl-independent; oligosaccharides

期刊名称：FRONTIERS IN MICROBIOLOGY （ 影响因子：5.64； 五年影响因子：6.32 ）

ISSN：

年卷期： 2021 年 12 卷

页码：

收录情况： SCI

摘要： Alginate lyase possesses wide application prospects for the degradation of brown algae and preparation of alginate oligosaccharides, and its degradation products display a variety of biological activities. Although many enzymes of this type have been reported, alginate lyases with unique properties are still relatively rare. In the present work, an alginate lyase abbreviated as Alyw203 has been cloned from Vibrio sp. W2 and expressed in food-grade Yarrowia lipolytica. The Alyw203 gene consists of an open reading frame (ORF) of 1,566 bp containing 521 amino acids, of which the first 17 amino acids are considered signal peptides, corresponding to secretory features. The peak activity of the current enzyme appears at 45 degrees C with a molecular weight of approximately 57.0 kDa. Interestingly, Alyw203 exhibits unique heat recovery performance, returning above 90% of its initial activity in the subsequent incubation for 20 min at 10 degrees C, which is conducive to the recovery of current enzymes at low-temperature conditions. Meanwhile, the highest activity is obtained under alkaline conditions of pH 10.0, showing outstanding pH stability. Additionally, as an alginate lyase independent of NaCl and resistant to metal ions, Alyw203 is highly active in various ionic environments. Moreover, the hydrolyzates of present enzymes are mainly concentrated in the oligosaccharides of DP1-DP2, displaying perfect product specificity. The alkali suitability, heat recovery performance, and high oligosaccharide yield of Alyw203 make it a potential candidate for industrial production of the monosaccharide and disaccharide.

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