Structural insights into curdlan degradation via a glycoside hydrolase containing a disruptive carbohydrate-binding module
© 2024. The Author(s)..
BACKGROUND: Degradation via enzymatic processes for the production of valuable β-1,3-glucooligosaccharides (GOS) from curdlan has attracted considerable interest. CBM6E functions as a curdlan-specific β-1,3-endoglucanase, composed of a glycoside hydrolase family 128 (GH128) module and a carbohydrate-binding module (CBM) derived from family CBM6.
RESULTS: Crystallographic analyses were conducted to comprehend the substrate specificity mechanism of CBM6E. This unveiled structures of both apo CBM6E and its GOS-complexed form. The GH128 and CBM6 modules constitute a cohesive unit, binding nine glucoside moieties within the catalytic groove in a singular helical conformation. By extending the substrate-binding groove, we engineered CBM6E variants with heightened hydrolytic activities, generating diverse GOS profiles from curdlan. Molecular docking, followed by mutation validation, unveiled the cooperative recognition of triple-helical β-1,3-glucan by the GH128 and CBM6 modules, along with the identification of a novel sugar-binding residue situated within the CBM6 module. Interestingly, supplementing the CBM6 module into curdlan gel disrupted the gel's network structure, enhancing the hydrolysis of curdlan by specific β-1,3-glucanases.
CONCLUSIONS: This study offers new insights into the recognition mechanism of glycoside hydrolases toward triple-helical β-1,3-glucans, presenting an effective method to enhance endoglucanase activity and manipulate its product profile. Furthermore, it discovered a CBM module capable of disrupting the quaternary structures of curdlan, thereby boosting the hydrolytic activity of curdlan gel when co-incubated with β-1,3-glucanases. These findings hold relevance for developing future enzyme and CBM cocktails useful in GOS production from curdlan degradation.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:17 |
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| Enthalten in: |
Biotechnology for biofuels and bioproducts - 17(2024), 1 vom: 21. März, Seite 45 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Lv, Tianhang [VerfasserIn] |
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| Links: |
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| Themen: |
β-1,3-Glucanase |
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| Anmerkungen: |
Date Revised 23.03.2024 published: Electronic Citation Status PubMed-not-MEDLINE |
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| doi: |
10.1186/s13068-024-02494-5 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM370047087 |
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| 520 | |a © 2024. The Author(s). | ||
| 520 | |a BACKGROUND: Degradation via enzymatic processes for the production of valuable β-1,3-glucooligosaccharides (GOS) from curdlan has attracted considerable interest. CBM6E functions as a curdlan-specific β-1,3-endoglucanase, composed of a glycoside hydrolase family 128 (GH128) module and a carbohydrate-binding module (CBM) derived from family CBM6 | ||
| 520 | |a RESULTS: Crystallographic analyses were conducted to comprehend the substrate specificity mechanism of CBM6E. This unveiled structures of both apo CBM6E and its GOS-complexed form. The GH128 and CBM6 modules constitute a cohesive unit, binding nine glucoside moieties within the catalytic groove in a singular helical conformation. By extending the substrate-binding groove, we engineered CBM6E variants with heightened hydrolytic activities, generating diverse GOS profiles from curdlan. Molecular docking, followed by mutation validation, unveiled the cooperative recognition of triple-helical β-1,3-glucan by the GH128 and CBM6 modules, along with the identification of a novel sugar-binding residue situated within the CBM6 module. Interestingly, supplementing the CBM6 module into curdlan gel disrupted the gel's network structure, enhancing the hydrolysis of curdlan by specific β-1,3-glucanases | ||
| 520 | |a CONCLUSIONS: This study offers new insights into the recognition mechanism of glycoside hydrolases toward triple-helical β-1,3-glucans, presenting an effective method to enhance endoglucanase activity and manipulate its product profile. Furthermore, it discovered a CBM module capable of disrupting the quaternary structures of curdlan, thereby boosting the hydrolytic activity of curdlan gel when co-incubated with β-1,3-glucanases. These findings hold relevance for developing future enzyme and CBM cocktails useful in GOS production from curdlan degradation | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Carbohydrate-binding module | |
| 650 | 4 | |a Curdlan | |
| 650 | 4 | |a Triple-helical β-1,3-glucan | |
| 650 | 4 | |a β-1,3-Glucanase | |
| 700 | 1 | |a Feng, Juanjuan |e verfasserin |4 aut | |
| 700 | 1 | |a Jia, Xiaoyu |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Cheng |e verfasserin |4 aut | |
| 700 | 1 | |a Li, Fudong |e verfasserin |4 aut | |
| 700 | 1 | |a Peng, Hui |e verfasserin |4 aut | |
| 700 | 1 | |a Xiao, Yazhong |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Lin |e verfasserin |4 aut | |
| 700 | 1 | |a He, Chao |e verfasserin |4 aut | |
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