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Home / Equine Research Bank / J Ind Microbiol Biotechnol / Metagenomic mining unveils a novel GH130 enzyme with exclusi...
Journal of industrial microbiology & biotechnology2025; 52; kuaf006; doi: 10.1093/jimb/kuaf006

Metagenomic mining unveils a novel GH130 enzyme with exclusive xylanase activity over a wide temperature and pH ranges.

Abstract: The equine gut harbors a diverse microbial community and represents a rich source of carbohydrate-active enzymes (CAZymes). To identify and characterize potentially novel CAZymes from a horse's hindgut metagenome, shotgun metagenomic sequencing was performed on DNA extracted from a stool sample of a male horse, followed by CAZyme annotation. Here, we report on the characterization of a novel enzyme (AH2) that was identified, synthesized, cloned, and characterized from the obtained CAZyme dataset. AH2 was identified as a GH130 family member and displayed exclusive xylanase activity, a trait hitherto unreported in prior characterization of GH130 CAZymes. AH2 displayed an optimal activity at a pH of 5.6 and a temperature of 50°C. AH2 maintained significant activity across a pH range of 4-10 (62-72%) and temperatures of 30-70°C (77-86%). The enzyme had remarkable stability, with minimal reductions in activity across a temperature range of 4-70°C and pH levels of 3, 7, and 9. Docking studies identified AH2's amino acids (Glu90 and Glu149) to be involved in substrate binding. Molecular dynamics simulation confirmed the structural stability of AH2 at pH 5.6 and 50°C, further supporting its resilience under these conditions. Our results expand on the known activities associated with the GH130 CAZyme family and demonstrate that the horse gut metagenome represents an unexplored source of novel CAZymes. Unassigned: A novel activity for members of the CAZyme family GH130.
© The Author(s) 2025. Published by Oxford University Press on behalf of Society of Industrial Microbiology and Biotechnology.
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Publication Date: 2025-03-04 PubMed ID: 40036345PubMed Central: PMC11905756DOI: 10.1093/jimb/kuaf006Google Scholar: Lookup
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  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research focuses on the discovery of a new enzyme, AH2, within a horse’s gut with a special capability to break down a particular type of carbohydrate. The enzyme, part of the GH130 CAZyme family, has a high-level of xylanase activity, making it unique and could be valuable in applications that require breaking down tough carbohydrates.

Understanding the Context

  • The gut of a horse was chosen for this study because of its ability to harbor an extensive range of microbial communities. The diversity of microorganisms makes the horse’s gut a rich source for isolating carbohydrate-active enzymes (CAZymes), which are key in breaking down carbohydrates.
  • The metagenomics approach used here involves sequencing DNA directly obtained from the horse’s stool sample. This allows for a comprehensive characterization of the microbial diversity present in the horse’s gut, leading to the discovery of new CAZymes such as AH2.

Study Findings and Methodology

  • The identified enzyme, AH2, belongs to the GH130 family of CAZymes. What makes AH2 unique is its exclusive xylanase activity, previously unreported for this family of enzymes. This ability allows it to break down xylans, a type of complex carbohydrate, more efficiently.
  • AH2 demonstrated optimal activity under specific environmental conditions: a pH of 5.6 and a temperature of 50°C. Surprisingly, the enzyme showed considerable resilience, maintaining its activity levels in a wide range of pH (4-10) and temperature (30-70°C) values.
  • The stability of AH2 was extremely impressive, with minimal reductions in activity even across a wide temperature range and different pH levels. This robustness could have significant benefits in its practical application, where varying environmental conditions often pose challenges.

Understanding AH2’s Mechanism

  • In order to understand how the enzyme functions, the researchers predicted amino acids (Glu90 and Glu149) that could be involved in substrate (the substance enzyme acts upon) binding. Further molecular dynamics simulations confirmed the enzyme’s structural stability, supporting its resilience under varying conditions.
  • The molecular docking and dynamics simulations also helped clarify the interactions between AH2 and its substrates, reinforcing the understanding about the enzyme’s function.

Significance of the Findings

  • The research has expanded the known activities of the GH130 CAZyme family. With AH2 displaying xylanase activity, new possibilities for using these enzymes to break down complex carbohydrates have emerged.
  • Moreover, the study highlights the horse gut metagenome as a potential untapped resource for isolating novel CAZymes, which can be beneficial in the development of new biotechnological tools and applications.

Cite This Article

APA
Hemeda AA, Zahran SA, Ali-Tammam M, Ewida MA, Kashef MT, Yassin AS, Mitra A, Youssef NH, Elshahed MS. (2025). Metagenomic mining unveils a novel GH130 enzyme with exclusive xylanase activity over a wide temperature and pH ranges. J Ind Microbiol Biotechnol, 52, kuaf006. https://doi.org/10.1093/jimb/kuaf006

Publication

Journal of industrial microbiology & biotechnology
ISSN: 1476-5535
NlmUniqueID: 9705544
Country: Germany
Language: English
Volume: 52
PII: kuaf006

Researcher Affiliations

Hemeda, Amr A
  • Department of Microbiology and Immunology, Faculty of Pharmacy, Future University in Egypt, 12311 Cairo, Egypt.
Zahran, Sara A
  • Department of Microbiology and Immunology, Faculty of Pharmacy, Future University in Egypt, 12311 Cairo, Egypt.
Ali-Tammam, Marwa
  • Department of Microbiology and Immunology, Faculty of Pharmacy, Future University in Egypt, 12311 Cairo, Egypt.
Ewida, Menna A
  • Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Future University in Egypt, 12311 Cairo, Egypt.
Kashef, Mona T
  • Department of Microbiology and Immunology, Faculty of Pharmacy, Cairo University, Cairo 11562, Egypt.
Yassin, Aymen S
  • Department of Microbiology and Immunology, Faculty of Pharmacy, Cairo University, Cairo 11562, Egypt.
Mitra, Avishek
  • Department of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, OK 74074, USA.
Youssef, Noha H
  • Department of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, OK 74074, USA.
Elshahed, Mostafa S
  • Department of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, OK 74074, USA.

MeSH Terms

  • Animals
  • Hydrogen-Ion Concentration
  • Temperature
  • Metagenomics
  • Enzyme Stability
  • Male
  • Horses
  • Metagenome
  • Molecular Dynamics Simulation
  • Feces / microbiology
  • Gastrointestinal Microbiome
  • Endo-1,4-beta Xylanases / genetics
  • Endo-1,4-beta Xylanases / metabolism
  • Endo-1,4-beta Xylanases / chemistry
  • Molecular Docking Simulation
  • Cloning, Molecular

Grant Funding

  • P20 GM134973 / NIGMS NIH HHS
  • P20 GM152333 / NIGMS NIH HHS
  • United States Agency for International Development
  • P20GM152333 / US National Institutes of Health
  • P20GM134973 / NIH HHS

Conflict of Interest Statement

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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