Biochemical Characterization and Cold-Adaption Mechanism of a PL-17 Family Alginate Lyase Aly23 from Marine Bacterium <i>Pseudoalteromonas</i> sp. ASY5 and Its Application for Oligosaccharides Production
As an important enzyme involved in the marine carbon cycle, alginate lyase has received extensive attention because of its excellent degradation ability on brown algae, which is widely utilized for alginate oligosaccharide preparation or bioethanol production. In comparison with endo-type alginate l...
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MDPI AG
2022-02-01
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| Series: | Marine Drugs |
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| Online Access: | https://www.mdpi.com/1660-3397/20/2/126 |
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| author | Xiang Tang Chao Jiao Yi Wei Xiao-Yan Zhuang Qiong Xiao Jun Chen Fu-Quan Chen Qiu-Ming Yang Hui-Fen Weng Bai-Shan Fang Yong-Hui Zhang An-Feng Xiao |
| author_facet | Xiang Tang Chao Jiao Yi Wei Xiao-Yan Zhuang Qiong Xiao Jun Chen Fu-Quan Chen Qiu-Ming Yang Hui-Fen Weng Bai-Shan Fang Yong-Hui Zhang An-Feng Xiao |
| author_sort | Xiang Tang |
| collection | DOAJ |
| description | As an important enzyme involved in the marine carbon cycle, alginate lyase has received extensive attention because of its excellent degradation ability on brown algae, which is widely utilized for alginate oligosaccharide preparation or bioethanol production. In comparison with endo-type alginate lyases (PL-5, PL-7, and PL-18 families), limited studies have focused on PL-17 family alginate lyases, especially for those with special characteristics. In this study, a novel PL-17 family alginate lyase, Aly23, was identified and cloned from the marine bacterium <i>Pseudoalteromonas carrageenovora</i> ASY5. Aly23 exhibited maximum activity at 35 °C and retained 48.93% of its highest activity at 4 °C, representing an excellent cold-adaptation property. Comparative molecular dynamics analysis was implemented to explore the structural basis for the cold-adaptation property of Aly23. Aly23 had a high substrate preference for poly β-D-mannuronate and exhibited both endolytic and exolytic activities; its hydrolysis reaction mainly produced monosaccharides, disaccharides, and trisaccharides. Furthermore, the enzymatic hydrolyzed oligosaccharides displayed good antioxidant activities to reduce ferric and scavenge radicals, such as hydroxyl, ABTS<sup>+</sup>, and DPPH. Our work demonstrated that Aly23 is a promising cold-adapted biocatalyst for the preparation of natural antioxidants from brown algae. |
| first_indexed | 2024-03-09T21:33:38Z |
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| language | English |
| last_indexed | 2024-03-09T21:33:38Z |
| publishDate | 2022-02-01 |
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| series | Marine Drugs |
| spelling | doaj.art-b7ec90de9aa94d2fbf6498fd9b679adf2023-11-23T20:50:16ZengMDPI AGMarine Drugs1660-33972022-02-0120212610.3390/md20020126Biochemical Characterization and Cold-Adaption Mechanism of a PL-17 Family Alginate Lyase Aly23 from Marine Bacterium <i>Pseudoalteromonas</i> sp. ASY5 and Its Application for Oligosaccharides ProductionXiang Tang0Chao Jiao1Yi Wei2Xiao-Yan Zhuang3Qiong Xiao4Jun Chen5Fu-Quan Chen6Qiu-Ming Yang7Hui-Fen Weng8Bai-Shan Fang9Yong-Hui Zhang10An-Feng Xiao11College of Food and Biological Engineering, Jimei University, Xiamen 361021, ChinaCollege of Food and Biological Engineering, Jimei University, Xiamen 361021, ChinaCollege of Food and Biological Engineering, Jimei University, Xiamen 361021, ChinaCollege of Food and Biological Engineering, Jimei University, Xiamen 361021, ChinaCollege of Food and Biological Engineering, Jimei University, Xiamen 361021, ChinaCollege of Food and Biological Engineering, Jimei University, Xiamen 361021, ChinaCollege of Food and Biological Engineering, Jimei University, Xiamen 361021, ChinaCollege of Food and Biological Engineering, Jimei University, Xiamen 361021, ChinaCollege of Food and Biological Engineering, Jimei University, Xiamen 361021, ChinaCollege of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361021, ChinaCollege of Food and Biological Engineering, Jimei University, Xiamen 361021, ChinaCollege of Food and Biological Engineering, Jimei University, Xiamen 361021, ChinaAs an important enzyme involved in the marine carbon cycle, alginate lyase has received extensive attention because of its excellent degradation ability on brown algae, which is widely utilized for alginate oligosaccharide preparation or bioethanol production. In comparison with endo-type alginate lyases (PL-5, PL-7, and PL-18 families), limited studies have focused on PL-17 family alginate lyases, especially for those with special characteristics. In this study, a novel PL-17 family alginate lyase, Aly23, was identified and cloned from the marine bacterium <i>Pseudoalteromonas carrageenovora</i> ASY5. Aly23 exhibited maximum activity at 35 °C and retained 48.93% of its highest activity at 4 °C, representing an excellent cold-adaptation property. Comparative molecular dynamics analysis was implemented to explore the structural basis for the cold-adaptation property of Aly23. Aly23 had a high substrate preference for poly β-D-mannuronate and exhibited both endolytic and exolytic activities; its hydrolysis reaction mainly produced monosaccharides, disaccharides, and trisaccharides. Furthermore, the enzymatic hydrolyzed oligosaccharides displayed good antioxidant activities to reduce ferric and scavenge radicals, such as hydroxyl, ABTS<sup>+</sup>, and DPPH. Our work demonstrated that Aly23 is a promising cold-adapted biocatalyst for the preparation of natural antioxidants from brown algae.https://www.mdpi.com/1660-3397/20/2/126alginate lyasePL-17 familycold-adaptedalginate oligosaccharides |
| spellingShingle | Xiang Tang Chao Jiao Yi Wei Xiao-Yan Zhuang Qiong Xiao Jun Chen Fu-Quan Chen Qiu-Ming Yang Hui-Fen Weng Bai-Shan Fang Yong-Hui Zhang An-Feng Xiao Biochemical Characterization and Cold-Adaption Mechanism of a PL-17 Family Alginate Lyase Aly23 from Marine Bacterium <i>Pseudoalteromonas</i> sp. ASY5 and Its Application for Oligosaccharides Production Marine Drugs alginate lyase PL-17 family cold-adapted alginate oligosaccharides |
| title | Biochemical Characterization and Cold-Adaption Mechanism of a PL-17 Family Alginate Lyase Aly23 from Marine Bacterium <i>Pseudoalteromonas</i> sp. ASY5 and Its Application for Oligosaccharides Production |
| title_full | Biochemical Characterization and Cold-Adaption Mechanism of a PL-17 Family Alginate Lyase Aly23 from Marine Bacterium <i>Pseudoalteromonas</i> sp. ASY5 and Its Application for Oligosaccharides Production |
| title_fullStr | Biochemical Characterization and Cold-Adaption Mechanism of a PL-17 Family Alginate Lyase Aly23 from Marine Bacterium <i>Pseudoalteromonas</i> sp. ASY5 and Its Application for Oligosaccharides Production |
| title_full_unstemmed | Biochemical Characterization and Cold-Adaption Mechanism of a PL-17 Family Alginate Lyase Aly23 from Marine Bacterium <i>Pseudoalteromonas</i> sp. ASY5 and Its Application for Oligosaccharides Production |
| title_short | Biochemical Characterization and Cold-Adaption Mechanism of a PL-17 Family Alginate Lyase Aly23 from Marine Bacterium <i>Pseudoalteromonas</i> sp. ASY5 and Its Application for Oligosaccharides Production |
| title_sort | biochemical characterization and cold adaption mechanism of a pl 17 family alginate lyase aly23 from marine bacterium i pseudoalteromonas i sp asy5 and its application for oligosaccharides production |
| topic | alginate lyase PL-17 family cold-adapted alginate oligosaccharides |
| url | https://www.mdpi.com/1660-3397/20/2/126 |
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