Discovery, structural characterization, and functional insights into a novel apiosidase from the GH140 family, isolated from a lignocellulolytic-enriched mangrove microbial community

Author(s)

Liberato, Marcelo Vizona ; Paixao, Douglas Antonio Alvaredo ; Tomazetto, Geizecler ; Ndeh, Didier ; Bolam, David N. ; Squina, Fabio Marcio

• Document type: Journal article
• Source: Biotechnology Letters; v. 46, n. 2, p. 11-pg., 2024-01-27.

Abstract

ObjectivesApiosidases are enzymes that cleave the glycosidic bond between the monosaccharides linked to apiose, a branched chain furanose found in the cell walls of vascular plants and aquatic monocots. There is biotechnological interest in this enzyme group because apiose is the flavor-active compound of grapes, fruit juice, and wine, and the monosaccharide is found to be a plant secondary metabolite with pharmaceutical properties. However, functional and structural studies of this enzyme family are scarce. Recently, a glycoside hydrolase family member GH140 was isolated from Bacteroides thetaiotaomicron and identified as an endo-apiosidase.ResultsThe structural characterization and functional identification of a second GH140 family enzyme, termed MmApi, discovered through mangrove soil metagenomic approach, are described. Among the various substrates tested, MmApi exhibited activity on an apiose-containing oligosaccharide derived from the pectic polysaccharide rhamnogalacturonan-II. While the crystallographic model of MmApi was similar to the endo-apiosidase from Bacteroides thetaiotaomicron, differences in the shape of the binding sites indicated that MmApi could cleave apioses within oligosaccharides of different compositions.ConclusionThis enzyme represents a novel tool for researchers interested in studying the physiology and structure of plant cell walls and developing biocatalytic strategies for drug and flavor production. (AU)

• FAPESP's process: 17/12597-2 - The structure and function of three multimodular glycoside hydrolases related to cellulose, hemicellulose and pectin breakdown, and the influence of the accessory modules in the catalytic activity.
• Grantee: Marcelo Vizoná Liberato
• Support Opportunities: Scholarships abroad - Research Internship - Post-doctor
• FAPESP's process: 14/04105-4 - Structural and functional characterization of new cellulases, focusing in the relation between catalytic domains and CBMs
• Grantee: Marcelo Vizoná Liberato
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• FAPESP's process: 20/05784-3 - EMU approved in grant 15 / 50590-4: chromatographic system and detectors for analysis of sugars and lignocellulosic monolignols
• Grantee: Fábio Márcio Squina
• Support Opportunities: Multi-user Equipment Program
• FAPESP's process: 22/08958-8 - Development of microorganisms and thermophilic enzymes involved in the degradation and upcycling of fossil plastics
• Grantee: Fábio Márcio Squina
• Support Opportunities: Regular Research Grants