Comparative studies of two AA10 family lytic polysaccharide monooxygenases from Bacillus thuringiensis
Bacillus thuringiensis, known to be one of the most important biocontrol microorganisms, contains three AA10 family lytic polysaccharide monooxygenases (LPMOs) in its genome. In previous reports, two of them, BtLPMO10A and BtLPMO10B, have been preliminarily characterized. However, some important bio...
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PeerJ Inc.
2023-01-01
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| author | Huiyan Zhang Haichuan Zhou Yong Zhao Tang Li Heng Yin |
| author_facet | Huiyan Zhang Haichuan Zhou Yong Zhao Tang Li Heng Yin |
| author_sort | Huiyan Zhang |
| collection | DOAJ |
| description | Bacillus thuringiensis, known to be one of the most important biocontrol microorganisms, contains three AA10 family lytic polysaccharide monooxygenases (LPMOs) in its genome. In previous reports, two of them, BtLPMO10A and BtLPMO10B, have been preliminarily characterized. However, some important biochemical features and substrate preference, as well as their potential applications in chitin degradation, still deserve further investigation. Results from present study showed that both BtLPMO10A and BtLPMO10B exhibit similar catalytic domains as well as highly conserved substrate-binding planes. However, unlike BtLPMO10A, which has comparable binding ability to both crystalline and amorphous form of chitins, BtLPMO10B exhibited much stronger binding ability to colloidal chitin, which mainly attribute to its carbohydrate-binding module-5 (CBM5). Interestingly, the relative high binding ability of BtLPMO10B to colloidal chitin does not lead to high catalytic activity of the enzyme. In contrast, the enzyme exhibited higher activity on β-chitin. Further experiments showed that the binding of BtLPMO10B to colloidal chitin was mainly non-productive, indicating a complicated role for CBM5 in LPMO activity. Furthermore, synergistic experiments demonstrated that both LPMOs boosted the activity of the chitinase, and the higher efficiency of BtLPMO10A can be overridden by BtLPMO10B. |
| first_indexed | 2024-03-09T07:00:25Z |
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| issn | 2167-8359 |
| language | English |
| last_indexed | 2024-03-09T07:00:25Z |
| publishDate | 2023-01-01 |
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| spelling | doaj.art-b94e7c1a2b93449295d53477eafa65c32023-12-03T09:53:01ZengPeerJ Inc.PeerJ2167-83592023-01-0111e1467010.7717/peerj.14670Comparative studies of two AA10 family lytic polysaccharide monooxygenases from Bacillus thuringiensisHuiyan Zhang0Haichuan Zhou1Yong Zhao2Tang Li3Heng Yin4Biotechnology Department, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, ChinaBiotechnology Department, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, ChinaBiotechnology Department, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, ChinaBiotechnology Department, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, ChinaBiotechnology Department, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, ChinaBacillus thuringiensis, known to be one of the most important biocontrol microorganisms, contains three AA10 family lytic polysaccharide monooxygenases (LPMOs) in its genome. In previous reports, two of them, BtLPMO10A and BtLPMO10B, have been preliminarily characterized. However, some important biochemical features and substrate preference, as well as their potential applications in chitin degradation, still deserve further investigation. Results from present study showed that both BtLPMO10A and BtLPMO10B exhibit similar catalytic domains as well as highly conserved substrate-binding planes. However, unlike BtLPMO10A, which has comparable binding ability to both crystalline and amorphous form of chitins, BtLPMO10B exhibited much stronger binding ability to colloidal chitin, which mainly attribute to its carbohydrate-binding module-5 (CBM5). Interestingly, the relative high binding ability of BtLPMO10B to colloidal chitin does not lead to high catalytic activity of the enzyme. In contrast, the enzyme exhibited higher activity on β-chitin. Further experiments showed that the binding of BtLPMO10B to colloidal chitin was mainly non-productive, indicating a complicated role for CBM5 in LPMO activity. Furthermore, synergistic experiments demonstrated that both LPMOs boosted the activity of the chitinase, and the higher efficiency of BtLPMO10A can be overridden by BtLPMO10B.https://peerj.com/articles/14670.pdfLytic polysaccharide monooxygenaseSynergyCBM5ChitinBacillus thuringiensis |
| spellingShingle | Huiyan Zhang Haichuan Zhou Yong Zhao Tang Li Heng Yin Comparative studies of two AA10 family lytic polysaccharide monooxygenases from Bacillus thuringiensis PeerJ Lytic polysaccharide monooxygenase Synergy CBM5 Chitin Bacillus thuringiensis |
| title | Comparative studies of two AA10 family lytic polysaccharide monooxygenases from Bacillus thuringiensis |
| title_full | Comparative studies of two AA10 family lytic polysaccharide monooxygenases from Bacillus thuringiensis |
| title_fullStr | Comparative studies of two AA10 family lytic polysaccharide monooxygenases from Bacillus thuringiensis |
| title_full_unstemmed | Comparative studies of two AA10 family lytic polysaccharide monooxygenases from Bacillus thuringiensis |
| title_short | Comparative studies of two AA10 family lytic polysaccharide monooxygenases from Bacillus thuringiensis |
| title_sort | comparative studies of two aa10 family lytic polysaccharide monooxygenases from bacillus thuringiensis |
| topic | Lytic polysaccharide monooxygenase Synergy CBM5 Chitin Bacillus thuringiensis |
| url | https://peerj.com/articles/14670.pdf |
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