Endogenous glycoside hydrolases reveal foraminiferal capacity to degrade terrestrial and marine polysaccharides

Foraminifera, a major component of sediment biomass, play a critical role in sedimentary food webs. In this study, we identified and characterized endogenous glycoside hydrolases (GHs) in Cymbaloporetta bradyi, demonstrating their capacity to degrade both terrestrial and marine polysaccharides. Through transcriptomic and in silico analyses, prokaryotic and eukaryotic contamination was minimized, ensuring the identified GHs were of foraminiferal origin. Our results revealed that cellulases, chitinases, and mannanases are the most highly expressed GHs, even under nutrient-rich conditions. Xylanases, pectinases, and fucosidases are also verified being possessed by C. bradyi. The presence of signal peptides in cellulases and cellulosome-related genes suggests an extracellular cellulose-degrading system in C. bradyi. These findings indicate that C. bradyi can metabolize polysaccharides from terrestrial plants and marine algae, reflecting adaptability to diverse sedimentary environments. As f..., , # Endogenous glycoside hydrolases reveal foraminiferal capacity to degrade terrestrial and marine polysaccharides

Dataset DOI: [10.5061/dryad.f1vhhmh72](10.5061/dryad.f1vhhmh72)

## Description of the data and file structure

This dataset contains the assembled transcripts of *C. bradyi*, and extracted transcripts that have similarities to cellulase, xylanase, pectinase, chitinase, mannanase, fucosidase, and laminarinase. 

### Files and variables

#### File: Assembled_transcripts_of_C.bradyi.fasta

**Description:** FASTA file containing assembled transcripts of *Cymbaloporetta bradyi*.

#### File: Annotation.csv

**Description:** Annotated transcripts analyzed by Trinotate, integraging BLASTp, Pfam(HMM), SignalP and Gene Ontology (GO) results.

| Column name | Definition |
| :---------------------- | :-------------------------------------------- |
| gene\_id | IDs of each gene generated by Trinity |
| transcript\_id...,