Thermophilic Hemicellulases Secreted by Microbial Consortia Selected from an Anaerobic Digester

Author:

Bombardi Luca1ORCID,Orlando Marco2ORCID,Aulitto Martina3ORCID,Fusco Salvatore1ORCID

Affiliation:

1. Biochemistry and Industrial Biotechnology (BIB) Laboratory, Department of Biotechnology, University of Verona, 37134 Verona, Italy

2. Department of Biotechnology and Biosciences, University of Milano Bicocca, 20126 Milano, Italy

3. Department of Biology, University of Naples Federico II, 80126 Naples, Italy

Abstract

The rise of agro-industrial activities over recent decades has exponentially increased lignocellulose biomasses (LCB) production. LCB serves as a cost-effective source for fermentable sugars and other renewable chemicals. This study explores the use of microbial consortia, particularly thermophilic consortia, for LCB deconstruction. Thermophiles produce stable enzymes that retain activity under industrial conditions, presenting a promising approach for LCB conversion. This research focused on two microbial consortia (i.e., microbiomes) that were analyzed for enzyme production using a cheap medium, i.e., a mixture of spent mushroom substrate (SMS) and digestate. The secreted xylanolytic enzymes were characterized in terms of temperature and pH optima, thermal stability, and hydrolysis products from LCB-derived polysaccharides. These enzymes showed optimal activity aligning with common biorefinery conditions and outperformed a formulated enzyme mixture in thermostability tests in the digestate. Phylogenetic and genomic analyses highlighted the genetic diversity and metabolic potential of these microbiomes. Bacillus licheniformis was identified as a key species, with two distinct strains contributing to enzyme production. The presence of specific glycoside hydrolases involved in the cellulose and hemicellulose degradation underscores these consortia’s capacity for efficient LCB conversion. These findings highlight the potential of thermophilic microbiomes, isolated from an industrial environment, as a robust source of robust enzymes, paving the way for more sustainable and cost-effective bioconversion processes in biofuel and biochemical production and other biotechnological applications.

Funder

MUR—Italian Ministry of University and Research

Next Generation EU

Publisher

MDPI AG

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