Characterization of a new bifunctional endo-1,4-beta-xylanase/esterase found in the rumen metagenome

Author(s)

Pavarina, Gabriella Cavazzini ^{[1, 2]} ; de Macedo Lemos, Eliana Gertrudes ^{[2, 3]} ; Monteiro Lima, Natalia Sarmanho ^{[1, 2]} ; Pizauro Jr, Joao Martins

Affiliation

^[1] Sao Paulo State Univ UNESP, Sch Agr & Vet Sci, Grad Program Agr & Livestock Microbiol, Jaboticabal, SP - Brazil

^[2] Sao Paulo State Univ Unesp, Sch Agr & Vet Sci, Technol Dept, Via Acesso Prof Paulo Donato Castellane S-N, Km 5, Sao Paulo - Brazil

^[3] Bioenergy Res Inst IPBEN, Mol Biol Lab, Jaboticabal, SP - Brazil

• Document type: Journal article
• Source: SCIENTIFIC REPORTS; v. 11, n. 1 MAY 17 2021.
• Web of Science Citations: 0

Abstract

Metagenomic data mining of the Nellore cattle rumen microbiota identified a new bifunctional enzyme, endo-1,4-beta -xylanase/esterase, which was subsequently overexpressed in E. coli BL21 (DE3). This enzyme was stable at pH intervals of 5 to 6.5 and temperatures between 30 and 45 degrees C, and under the test conditions, it had a V-max of 30.959 +/- 2.334 mu mol/min/mg, K-m of 3.6 +/- 0.6 mM and k(cat) of 2.323 +/- 175 s(-1). Additionally, the results showed that the enzyme is tolerant to NaCl and organic solvents and therefore is suitable for industrial environments. Xylanases are widely applicable, and the synergistic activity of endo-1,4-beta -xylanase/esterase in a single molecule will improve the degradation efficiency of heteroxylans via the creation of xylanase binding sites. Therefore, this new molecule has the potential for use in lignocellulosic biomass processing and as an animal feed food additive and could improve xylooligosaccharide production efficiency. (AU)

• FAPESP's process: 18/12885-0 - Prospecting, heterologous expression, purification and characterization of a xylanase
• Grantee: Gabriella Cavazzini Pavarina
• Support Opportunities: Scholarships in Brazil - Master