Elucidation of a Unique Pattern and the Role of Carbohydrate Binding Module of an Alginate Lyase
Alginate oligosaccharides with different degrees of polymerization (DPs) possess diverse physiological activities. Therefore, in recent years, increasing attention has been drawn to the use of enzymes for the preparation of alginate oligosaccharides for food and industrial applications. Previously,...
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| Format: | Article |
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MDPI AG
2019-12-01
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| Series: | Marine Drugs |
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| Online Access: | https://www.mdpi.com/1660-3397/18/1/32 |
| _version_ | 1828119155032719360 |
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| author | Fu Hu Benwei Zhu Qian Li Heng Yin Yun Sun Zhong Yao Dengming Ming |
| author_facet | Fu Hu Benwei Zhu Qian Li Heng Yin Yun Sun Zhong Yao Dengming Ming |
| author_sort | Fu Hu |
| collection | DOAJ |
| description | Alginate oligosaccharides with different degrees of polymerization (DPs) possess diverse physiological activities. Therefore, in recent years, increasing attention has been drawn to the use of enzymes for the preparation of alginate oligosaccharides for food and industrial applications. Previously, we identified and characterized a novel bifunctional alginate lyase Aly7A, which can specifically release trisaccharide from three different substrate types with a unique degradation pattern. Herein, we investigated its degradation pattern by modular truncation and molecular docking. The results suggested that Aly7A adopted a unique action mode towards different substrates with the substrate chain sliding into the binding pocket of the catalytic domain to position the next trisaccharide for cleavage. Deletion of the Aly7A carbohydrate binding module (CBM) domain resulted in a complex distribution of degradation products and no preference for trisaccharide formation, indicating that the CBM may act as a “controller” during the trisaccharide release process. This study further testifies CBM as a regulator of product distribution and provides new insights into well-defined generation of alginate oligosaccharides with associated CBMs. |
| first_indexed | 2024-04-11T13:43:34Z |
| format | Article |
| id | doaj.art-f503061914fb4032ada8835c1f3b0d0b |
| institution | Directory Open Access Journal |
| issn | 1660-3397 |
| language | English |
| last_indexed | 2024-04-11T13:43:34Z |
| publishDate | 2019-12-01 |
| publisher | MDPI AG |
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| series | Marine Drugs |
| spelling | doaj.art-f503061914fb4032ada8835c1f3b0d0b2022-12-22T04:21:10ZengMDPI AGMarine Drugs1660-33972019-12-011813210.3390/md18010032md18010032Elucidation of a Unique Pattern and the Role of Carbohydrate Binding Module of an Alginate LyaseFu Hu0Benwei Zhu1Qian Li2Heng Yin3Yun Sun4Zhong Yao5Dengming Ming6College of Food Science and Light Industry, Nanjing Tech University, Nanjing 211816, ChinaCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing 211816, ChinaCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing 211816, ChinaDalian Institute of Chemical Physics, Chinese Academy of Sciences, CAS, Dalian 116023, ChinaCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing 211816, ChinaCollege of Food Science and Light Industry, Nanjing Tech University, Nanjing 211816, ChinaCollege of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211816, ChinaAlginate oligosaccharides with different degrees of polymerization (DPs) possess diverse physiological activities. Therefore, in recent years, increasing attention has been drawn to the use of enzymes for the preparation of alginate oligosaccharides for food and industrial applications. Previously, we identified and characterized a novel bifunctional alginate lyase Aly7A, which can specifically release trisaccharide from three different substrate types with a unique degradation pattern. Herein, we investigated its degradation pattern by modular truncation and molecular docking. The results suggested that Aly7A adopted a unique action mode towards different substrates with the substrate chain sliding into the binding pocket of the catalytic domain to position the next trisaccharide for cleavage. Deletion of the Aly7A carbohydrate binding module (CBM) domain resulted in a complex distribution of degradation products and no preference for trisaccharide formation, indicating that the CBM may act as a “controller” during the trisaccharide release process. This study further testifies CBM as a regulator of product distribution and provides new insights into well-defined generation of alginate oligosaccharides with associated CBMs.https://www.mdpi.com/1660-3397/18/1/32alginate lyasetrisaccharide preparationdegrading patternunique mechanismoligosaccharides |
| spellingShingle | Fu Hu Benwei Zhu Qian Li Heng Yin Yun Sun Zhong Yao Dengming Ming Elucidation of a Unique Pattern and the Role of Carbohydrate Binding Module of an Alginate Lyase Marine Drugs alginate lyase trisaccharide preparation degrading pattern unique mechanism oligosaccharides |
| title | Elucidation of a Unique Pattern and the Role of Carbohydrate Binding Module of an Alginate Lyase |
| title_full | Elucidation of a Unique Pattern and the Role of Carbohydrate Binding Module of an Alginate Lyase |
| title_fullStr | Elucidation of a Unique Pattern and the Role of Carbohydrate Binding Module of an Alginate Lyase |
| title_full_unstemmed | Elucidation of a Unique Pattern and the Role of Carbohydrate Binding Module of an Alginate Lyase |
| title_short | Elucidation of a Unique Pattern and the Role of Carbohydrate Binding Module of an Alginate Lyase |
| title_sort | elucidation of a unique pattern and the role of carbohydrate binding module of an alginate lyase |
| topic | alginate lyase trisaccharide preparation degrading pattern unique mechanism oligosaccharides |
| url | https://www.mdpi.com/1660-3397/18/1/32 |
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