Frontiers in Microbiology (Jan 2022)
The Function of CBM32 in Alginate Lyase VxAly7B on the Activity on Both Soluble Sodium Alginate and Alginate Gel
- Luyao Tang,
- Luyao Tang,
- Luyao Tang,
- Luyao Tang,
- Enwen Guo,
- Enwen Guo,
- Enwen Guo,
- Enwen Guo,
- Lan Zhang,
- Lan Zhang,
- Lan Zhang,
- Lan Zhang,
- Ying Wang,
- Ying Wang,
- Ying Wang,
- Ying Wang,
- Shan Gao,
- Shan Gao,
- Shan Gao,
- Shan Gao,
- Mengmeng Bao,
- Mengmeng Bao,
- Mengmeng Bao,
- Mengmeng Bao,
- Feng Han,
- Feng Han,
- Feng Han,
- Feng Han,
- Wengong Yu,
- Wengong Yu,
- Wengong Yu,
- Wengong Yu
Affiliations
- Luyao Tang
- School of Medicine and Pharmacy, Ocean University of China, Qingdao, China
- Luyao Tang
- Key Laboratory of Marine Drugs, Ministry of Education, Qingdao, China
- Luyao Tang
- Shandong Provincial Key Laboratory of Glycoscience and Glycoengineering, Qingdao, China
- Luyao Tang
- Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao, China
- Enwen Guo
- School of Medicine and Pharmacy, Ocean University of China, Qingdao, China
- Enwen Guo
- Key Laboratory of Marine Drugs, Ministry of Education, Qingdao, China
- Enwen Guo
- Shandong Provincial Key Laboratory of Glycoscience and Glycoengineering, Qingdao, China
- Enwen Guo
- Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao, China
- Lan Zhang
- School of Medicine and Pharmacy, Ocean University of China, Qingdao, China
- Lan Zhang
- Key Laboratory of Marine Drugs, Ministry of Education, Qingdao, China
- Lan Zhang
- Shandong Provincial Key Laboratory of Glycoscience and Glycoengineering, Qingdao, China
- Lan Zhang
- Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao, China
- Ying Wang
- School of Medicine and Pharmacy, Ocean University of China, Qingdao, China
- Ying Wang
- Key Laboratory of Marine Drugs, Ministry of Education, Qingdao, China
- Ying Wang
- Shandong Provincial Key Laboratory of Glycoscience and Glycoengineering, Qingdao, China
- Ying Wang
- Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao, China
- Shan Gao
- School of Medicine and Pharmacy, Ocean University of China, Qingdao, China
- Shan Gao
- Key Laboratory of Marine Drugs, Ministry of Education, Qingdao, China
- Shan Gao
- Shandong Provincial Key Laboratory of Glycoscience and Glycoengineering, Qingdao, China
- Shan Gao
- Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao, China
- Mengmeng Bao
- School of Medicine and Pharmacy, Ocean University of China, Qingdao, China
- Mengmeng Bao
- Key Laboratory of Marine Drugs, Ministry of Education, Qingdao, China
- Mengmeng Bao
- Shandong Provincial Key Laboratory of Glycoscience and Glycoengineering, Qingdao, China
- Mengmeng Bao
- Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao, China
- Feng Han
- School of Medicine and Pharmacy, Ocean University of China, Qingdao, China
- Feng Han
- Key Laboratory of Marine Drugs, Ministry of Education, Qingdao, China
- Feng Han
- Shandong Provincial Key Laboratory of Glycoscience and Glycoengineering, Qingdao, China
- Feng Han
- Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao, China
- Wengong Yu
- School of Medicine and Pharmacy, Ocean University of China, Qingdao, China
- Wengong Yu
- Key Laboratory of Marine Drugs, Ministry of Education, Qingdao, China
- Wengong Yu
- Shandong Provincial Key Laboratory of Glycoscience and Glycoengineering, Qingdao, China
- Wengong Yu
- Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao, China
- DOI
- https://doi.org/10.3389/fmicb.2021.798819
- Journal volume & issue
-
Vol. 12
Abstract
Carbohydrate-binding modules (CBMs), as an important auxiliary module, play a key role in degrading soluble alginate by alginate lyase, but the function on alginate gel has not been elucidated. Recently, we reported alginate lyase VxAly7B containing a CBM32 and a polysaccharide lyase family 7 (PL7). To investigate the specific function of CBM32, we characterized the full-length alginate lyase VxAly7B (VxAly7B-FL) and truncated mutants VxAly7B-CM (PL7) and VxAly7B-CBM (CBM32). Both VxAly7B-FL and native VxAly7B can spontaneously cleavage between CBM32 and PL7. The substrate-binding capacity and activity of VxAly7B-CM to soluble alginate were 0.86- and 1.97-fold those of VxAly7B-FL, respectively. Moreover, CBM32 could accelerate the expansion and cleavage of alginate gel beads, and the degradation rate of VxAly7B-FL to alginate gel beads was threefold that of VxAly7B-CM. Results showed that CBM32 is not conducive to the degradation of soluble alginate by VxAly7B but is helpful for binding and degradation of insoluble alginate gel. This study provides new insights into the function of CBM32 on alginate gel, which may inspire the application strategy of CBMs in insoluble substrates.
Keywords
- alginate lyase
- alginate gel
- insoluble substrate
- carbohydrate-binding module (CBM)
- binding capacity
- function
