Expression and Characterization of a Cold-Adapted Alginate Lyase with Exo/Endo-Type Activity from a Novel Marine Bacterium <i>Alteromonas portus</i> HB161718<sup>T</sup>
The alginate lyases have unique advantages in the preparation of alginate oligosaccharides and processing of brown algae. Herein, a gene <i>alg2951</i> encoding a PL7 family alginate lyase with exo/endo-type activity was cloned from a novel marine bacterium <i>Alteromonas portus<...
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MDPI AG
2021-03-01
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| Series: | Marine Drugs |
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| Online Access: | https://www.mdpi.com/1660-3397/19/3/155 |
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| author | Huiqin Huang Shuang Li Shixiang Bao Kunlian Mo Dongmei Sun Yonghua Hu |
| author_facet | Huiqin Huang Shuang Li Shixiang Bao Kunlian Mo Dongmei Sun Yonghua Hu |
| author_sort | Huiqin Huang |
| collection | DOAJ |
| description | The alginate lyases have unique advantages in the preparation of alginate oligosaccharides and processing of brown algae. Herein, a gene <i>alg2951</i> encoding a PL7 family alginate lyase with exo/endo-type activity was cloned from a novel marine bacterium <i>Alteromonas portus</i> HB161718<sup>T</sup> and then expressed in <i>Escherichia coli</i>. 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 °C and pH 8.0, was relatively stable at temperatures lower than 30 °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. |
| first_indexed | 2024-03-10T13:10:41Z |
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| institution | Directory Open Access Journal |
| issn | 1660-3397 |
| language | English |
| last_indexed | 2024-03-10T13:10:41Z |
| publishDate | 2021-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj.art-f04912bc8bc2462a8262e9252ac8d1b22023-11-21T10:47:42ZengMDPI AGMarine Drugs1660-33972021-03-0119315510.3390/md19030155Expression and Characterization of a Cold-Adapted Alginate Lyase with Exo/Endo-Type Activity from a Novel Marine Bacterium <i>Alteromonas portus</i> HB161718<sup>T</sup>Huiqin Huang0Shuang Li1Shixiang Bao2Kunlian Mo3Dongmei Sun4Yonghua Hu5Institute of Tropical Bioscience and Biotechnology, Hainan Institute for Tropical Agricultural Resources, CATAS, Haikou 571101, ChinaInstitute of Tropical Bioscience and Biotechnology, Hainan Institute for Tropical Agricultural Resources, CATAS, Haikou 571101, ChinaInstitute of Tropical Bioscience and Biotechnology, Hainan Institute for Tropical Agricultural Resources, CATAS, Haikou 571101, ChinaInstitute of Tropical Bioscience and Biotechnology, Hainan Institute for Tropical Agricultural Resources, CATAS, Haikou 571101, ChinaCollege of Life Science and Technology, Heilongjiang Bayi Agricultural University, Daqing 163000, ChinaInstitute of Tropical Bioscience and Biotechnology, Hainan Institute for Tropical Agricultural Resources, CATAS, Haikou 571101, ChinaThe alginate lyases have unique advantages in the preparation of alginate oligosaccharides and processing of brown algae. Herein, a gene <i>alg2951</i> encoding a PL7 family alginate lyase with exo/endo-type activity was cloned from a novel marine bacterium <i>Alteromonas portus</i> HB161718<sup>T</sup> and then expressed in <i>Escherichia coli</i>. 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 °C and pH 8.0, was relatively stable at temperatures lower than 30 °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.https://www.mdpi.com/1660-3397/19/3/155alginate lyasecold-adaptedexo/endo-type<i>Alteromonas portus</i>oligosaccharideantioxidant activity |
| spellingShingle | Huiqin Huang Shuang Li Shixiang Bao Kunlian Mo Dongmei Sun Yonghua Hu Expression and Characterization of a Cold-Adapted Alginate Lyase with Exo/Endo-Type Activity from a Novel Marine Bacterium <i>Alteromonas portus</i> HB161718<sup>T</sup> Marine Drugs alginate lyase cold-adapted exo/endo-type <i>Alteromonas portus</i> oligosaccharide antioxidant activity |
| title | Expression and Characterization of a Cold-Adapted Alginate Lyase with Exo/Endo-Type Activity from a Novel Marine Bacterium <i>Alteromonas portus</i> HB161718<sup>T</sup> |
| title_full | Expression and Characterization of a Cold-Adapted Alginate Lyase with Exo/Endo-Type Activity from a Novel Marine Bacterium <i>Alteromonas portus</i> HB161718<sup>T</sup> |
| title_fullStr | Expression and Characterization of a Cold-Adapted Alginate Lyase with Exo/Endo-Type Activity from a Novel Marine Bacterium <i>Alteromonas portus</i> HB161718<sup>T</sup> |
| title_full_unstemmed | Expression and Characterization of a Cold-Adapted Alginate Lyase with Exo/Endo-Type Activity from a Novel Marine Bacterium <i>Alteromonas portus</i> HB161718<sup>T</sup> |
| title_short | Expression and Characterization of a Cold-Adapted Alginate Lyase with Exo/Endo-Type Activity from a Novel Marine Bacterium <i>Alteromonas portus</i> HB161718<sup>T</sup> |
| title_sort | expression and characterization of a cold adapted alginate lyase with exo endo type activity from a novel marine bacterium i alteromonas portus i hb161718 sup t sup |
| topic | alginate lyase cold-adapted exo/endo-type <i>Alteromonas portus</i> oligosaccharide antioxidant activity |
| url | https://www.mdpi.com/1660-3397/19/3/155 |
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