Functional and computational analysis of a recombinant lytic polysaccharide monooxygenase (LPMO) from the thermotolerant fungus Aspergillus fumigatus var. niveus (2024)
- Authors:
- USP affiliated authors: SEGATO, FERNANDO - EEL ; ARAGÃO, MATHEUS ITALO BOMFIM - EEL ; CONTATO, ALEX GRAÇA - EEL ; BERTO, GABRIELA LEILA - EEL
- Unidade: EEL
- Subjects: BIOQUÍMICA; ASPERGILLUS
- Keywords: biochemical characterization; lytic polysaccharide monooxygenases; Aspergillus fumigatus var. niveus
- Agências de fomento:
- Language: Inglês
- Abstract: Lytic polysaccharide monooxygenases (LPMOs) are auxiliary activity (AA) enzymes that can potentiate the action of glycosyl hydrolases (GH) by introducing breaks in the crystalline chain of cellulose by oxidatively action and thus reducing its recalcitrance. Although the contribution of additional factors and oxidative enzymes has been predicted since the 1950s, the existence and structure of LPMOs have only recently been described. These proteins are metalloenzymes classified into eight specific AA families (9, 10, 11, 13, 14, 15, 16 and 17), accordingly to Carbohydrate Activity enZymes database (CAZy). LPMOs catalyze the oxidative cleavage of the β-(1,4) glycosidic bonds of the cellulose chain using reactive oxygen species to abstract a C1, C4 or C1/C4 hydrogen from the glucose ring, followed by hydroxylation of the substrate at these positions. LPMOs have activity against a variety of polymeric substrates, including cellulose, starch, or chitin. LPMOs from the AA9 family may also show promiscuous activity against hemicelluloses such as β-glucan, glucomannan, xylan and xyloglucan. In this work, a gene encoding an Aspergillus fumigatus var. niveus LPMO containing a disordered C-terminal Region (dCTR) was cloned and successfully expressed in Aspergillus nidulans strain A773. The purification of the protein was performed in two steps: ion exchange and size exclusion chromatography. The protein fractions were collected and analyzed with SDSPAGE. After, we performed the characterization in relationship optimum pH and temperature, thermostability and pH stability and regioselectivity by high-performance anion-exchange chromatography with amperometric detector (HPAEC-PAD). The last step was to perform molecular modeling of the LPMO by computational methods as well as to complement the utilization of LPMOs in the enzymatic saccharification of lignocellulosic biomass.
- Imprenta:
- Publisher: UFMG
- Publisher place: Belo Horizonte-MG
- Date published: 2024
- Source:
- Título: Anais do X Congresso Brasileiro de Microbiologia
- Volume/Número/Paginação/Ano: art. n. 324, p.436, 2024
-
ABNT
CONTATO, Alex Graça et al. Functional and computational analysis of a recombinant lytic polysaccharide monooxygenase (LPMO) from the thermotolerant fungus Aspergillus fumigatus var. niveus. 2024, Anais.. Belo Horizonte-MG: UFMG, 2024. p. 436. Disponível em: https://www.cbmic2024.com.br/files/anaisfinal.pdf. Acesso em: 04 ago. 2025. -
APA
Contato, A. G., Aragao, M. I. B., Berto, G. L., & Segato, F. (2024). Functional and computational analysis of a recombinant lytic polysaccharide monooxygenase (LPMO) from the thermotolerant fungus Aspergillus fumigatus var. niveus. In Anais do X Congresso Brasileiro de Microbiologia (p. 436). Belo Horizonte-MG: UFMG. Recuperado de https://www.cbmic2024.com.br/files/anaisfinal.pdf -
NLM
Contato AG, Aragao MIB, Berto GL, Segato F. Functional and computational analysis of a recombinant lytic polysaccharide monooxygenase (LPMO) from the thermotolerant fungus Aspergillus fumigatus var. niveus [Internet]. Anais do X Congresso Brasileiro de Microbiologia. 2024 ;(art. 324): 436.[citado 2025 ago. 04 ] Available from: https://www.cbmic2024.com.br/files/anaisfinal.pdf -
Vancouver
Contato AG, Aragao MIB, Berto GL, Segato F. Functional and computational analysis of a recombinant lytic polysaccharide monooxygenase (LPMO) from the thermotolerant fungus Aspergillus fumigatus var. niveus [Internet]. Anais do X Congresso Brasileiro de Microbiologia. 2024 ;(art. 324): 436.[citado 2025 ago. 04 ] Available from: https://www.cbmic2024.com.br/files/anaisfinal.pdf - Thermothelomyces thermophilus as industrial cell factory for high titter of biomoleculaes production
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