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
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

129978

Informations 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.

Auteurs

Yaojing Qiu (Y)

Department of Biological Systems Engineering, Washington State University, Pullman, WA 99164-6120, United States.

Zachary Johnson (Z)

Department of Biological Systems Engineering, Washington State University, Pullman, WA 99164-6120, United States; Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99354, United States.

Xiangyu Gu (X)

State Key laboratory of Multiphase Complex Systems, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China.

Pavlo Bohutskyi (P)

Department of Biological Systems Engineering, Washington State University, Pullman, WA 99164-6120, United States; Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99354, United States. Electronic address: pavlo.bohutskyi@pnnl.gov.

Shulin Chen (S)

Department of Biological Systems Engineering, Washington State University, Pullman, WA 99164-6120, United States. Electronic address: chens@wsu.edu.

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