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Development of a rapid assay for β-etherase activity using a novel chromogenic substrate

Talanta. 2023-12; 
Itzel Celeste Romero-Soto, Jorge A Rodríguez, Vicente Paúl Armenta-Pérez, Raúl Balam Martínez-Pérez, Rosa María Camacho-Ruiz, Leociley Rocha Alencar Menezes, Guilherme Lanzi Sassaki, Arquimedes Santana-Filho, María Angeles Camacho-Ruiz
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Codon Optimization … B11 were synthesized by GenScript (USA) with codon optimization for E. coli and cloned into … [7] was 0.086 s ?1 mM ?1 (calculated from the values they reported for K CAT and K M ) for … Get A Quote

摘要

Biocatalytic processes play a crucial role in the valorization of lignin; therefore, methods enabling the monitoring of enzymes such as β-etherases, capable of breaking β-O-4 aryl-ether bonds, are of significant biotechnological interest. A novel method for quantifying β-etherase activity was developed based on the β-ester bond formation between a chromophore and acetovainillone. The chromogenic substrate β-(ρ-nitrophenoxy)-α-acetovanillone (PNPAV), was chemically synthesized. Kintetic monitoring of ρ-nitrophenolate release at 410?nm over 10?min, using recombinant LigF from Sphingobium sp SYK-6, LigF-AB and LigE-AB from Althererytrobacter sp B11, yielded enzimatic activities of 404. 3 mU/mg, 72 mU/mg,... More

關鍵詞

Chromogenic substrate, Kinetic method, Lignin, β-(ρ-nitrophenoxy)-α-acetovanillone), β-etherase
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