Dairy manure acidogenic fermentation at hyperthermophilic temperature enabled superior activity of thermostable hydrolytic enzymes linked to the genus Caldicoprobacter.
Cellulolytic activity
Evolving enhanced hydrolytic activity
Hemicellulolytic activity
Proteolytic activity
Thermostable hydrolases
Journal
Bioresource technology
ISSN: 1873-2976
Titre abrégé: Bioresour Technol
Pays: England
ID NLM: 9889523
Informations de publication
Date de publication:
Jan 2024
Jan 2024
Historique:
received:
25
07
2023
revised:
01
11
2023
accepted:
01
11
2023
medline:
24
11
2023
pubmed:
10
11
2023
entrez:
9
11
2023
Statut:
ppublish
Résumé
In this study, fermentation experiments were conducted under mesophilic, thermophilic, and hyperthermophilic conditions to investigate adaptation of microbial communities and its effect on extracellular enzyme activities toward degradation of cellulose, hemicellulose and proteins in dairy manure. Hyperthermophilic conditions transformed the microbiome structure and stimulated activity of extracellular proteolytic, cellulolytic, and hemicellulolytic enzymes. Specifically, the activities of protease, cellulose 1,4-β-cellobiosidase, and β-glucosidase secreted by hyperthermophilic microbes were higher by 22%, 47% and 49% compared to those produced by mesophilic and thermophilic communities. Enhanced hydrolytic activity of hyperthermophilic microbes enabled improved feedstock solubilization and production of 39% and 22% more soluble COD than mesophilic and thermophilic microbes, respectively. Connections between hydrolytic function and microbial community structure at various temperatures were assessed using the PICRUSt2 computational tool. Genus Caldicoprobacter was identified as the primary candidate responsible for increased production of thermostable endo-1,4-β-glucanase, β-glucosidase and endo-1,4-β-xylanase, and enhanced hydrolytic performance of hyperthermophilic microbial community.
Identifiants
pubmed: 37944622
pii: S0960-8524(23)01406-2
doi: 10.1016/j.biortech.2023.129978
pii:
doi:
Substances chimiques
Manure
0
Cellulose
9004-34-6
Acids
0
Cellulases
EC 3.2.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
129978Informations de copyright
Published by Elsevier Ltd.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Shulin Chen reports financial support was provided by US Department of Energy. Yaojing Qiu reports a relationship with China Scholarship Council that includes: funding grants.