Expression and Characterization of a Cold-Adapted Alginate Lyase with Exo/Endo-Type Activity from a Novel Marine Bacterium Alteromonas portus HB161718(T)
文献类型： 外文期刊
作者： Huang, Huiqin 1 ; Li, Shuang 1 ; Bao, Shixiang 1 ; Mo, Kunlian 1 ; Sun, Dongmei 3 ; Hu, Yonghua 1 ;
作者机构： 1.Inst Trop Biosci & Biotechnol, Hainan Inst Trop Agr Resources, CATAS, Haikou 571101, Hainan, Peoples R China
2.Hainan Prov Key Lab Funct Components Res & Utiliz, Haikou 571101, Hainan, Peoples R China
3.Heilongjiang Bayi Agr Univ, Coll Life Sci & Technol, Daqing 163000, Peoples R China
4.Pilot Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao 266071, Peoples R China
关键词： alginate lyase; cold-adapted; exo; endo-type; Alteromonas portus; oligosaccharide; antioxidant activity
期刊名称：MARINE DRUGS （ 影响因子：4.073； 五年影响因子：4.877 ）
ISSN：
年卷期： 2021 年 19 卷 3 期
页码：
收录情况： SCI
摘要： The alginate lyases have unique advantages in the preparation of alginate oligosaccharides and processing of brown algae. Herein, a gene alg2951 encoding a PL7 family alginate lyase with exo/endo-type activity was cloned from a novel marine bacterium Alteromonas portus HB161718(T) and then expressed in Escherichia coli. The recombinant Alg2951 in the culture supernatant reached the activity of 63.6 U/mL, with a molecular weight of approximate 60 kDa. Alg2951 exhibited the maximum activity at 25 degrees C and pH 8.0, was relatively stable at temperatures lower than 30 degrees C, and showed a special preference to poly-guluronic acid (polyG) as well. Both NaCl and KCl had the most promotion effect on the enzyme activity of Alg2951 at 0.2 M, increasing by 21.6 and 19.1 times, respectively. The TCL (Thin Layer Chromatography) and ESI-MS (Electrospray Ionization Mass Spectrometry) analyses suggested that Alg2951 could catalyze the hydrolysis of sodium alginate to produce monosaccharides and trisaccharides. Furthermore, the enzymatic hydrolysates displayed good antioxidant activity by assays of the scavenging abilities towards radicals (hydroxyl and ABTS+) and the reducing power. Due to its cold-adapted and dual exo/endo-type properties, Alg2951 can be a potential enzymatic tool for industrial production.
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