Effect of LPMO on the Hydrolysis of Crystalline Chitin by Chitinase A and β-<em>N</em>-Acetylglucosaminidase from <em>Paenibacillus</em> sp.
We performed cloning and expression of chitinase A (Pb-ChiA), β-GlcNAcase (Pb-GlcNAcase), and lytic polysaccharide monooxygenase (Pb-LPMO) genes from Paenibacillus sp. The analysis of the hydrolysis products indicated Pb-ChiA to be an exo-type chitinase with 10-fold activity toward β-chitin as compa...
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| Autores principales: | , , , |
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| Formato: | Capítulo de libro |
| Lenguaje: | inglés |
| Publicado: |
IntechOpen
2020
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| Materias: | |
| Acceso en línea: | https://www.intechopen.com/chapters/73409 |
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| Sumario: | We performed cloning and expression of chitinase A (Pb-ChiA), β-GlcNAcase (Pb-GlcNAcase), and lytic polysaccharide monooxygenase (Pb-LPMO) genes from Paenibacillus sp. The analysis of the hydrolysis products indicated Pb-ChiA to be an exo-type chitinase with 10-fold activity toward β-chitin as compared with α-chitin. The sequence of Pb-GlcNAcase was found to be similar to that of β-N-acetylhexosaminidase from P. barengoltzii (99%, WP_016313754.1). Pb-LPMO was expressed in the Brevibacillus expression system. Pb-ChiA was found to have affinity toward crystalline chitin higher than that of Pb-LPMO. Pb-LPMO boosted the activity of Pb-ChiA toward crystalline α-chitin but not toward crystalline β-chitin. When Pb-LPMO (3 μM) was added to the reaction mixture during the hydrolysis of crystalline α-chitin by Pb-ChiA, hydrolysis products at two-fold concentration were obtained. However, the hydrolysis products decreased upon addition of more than 3 μM Pb-LPMO to the reaction mixture. |
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| ISBN: | 978-1-83880-797-9 |
| DOI: | 10.5772/intechopen.93761 |