Mining and Characterization of Carbohydrate-Active Enzymes in MAGs from Animal Gut Microbes
- 1College of Life Sciences, Shihezi University, Shihezi 832003, China
- 2College of Grassland Science, Xinjiang Agricultural University, Urumqi 830052, China
Abstract
Background: CAZymes mediate carbohydrate catabolism in animals and are critical for supporting animal growth, development, metabolism and production performance. This study aimed to explore the gut microbial CAZyme repertoire of humans and multiple animal species and identify novel and efficient CAZymes. Methods: A total of 100,090 MAGs from humans and 10 animal species were collected for CAZyme annotation. PULpy was used to annotates PULs encoded by the Bacteroides. DeepFRI annotation combined with molecular docking was used to screen novel CAZymes. Prokaryotic expression was further performed to obtain the target enzyme and verify its substrate-degrading activity. Results: We annotated 8,747,365 known CAZymes spanning 613 carbohydrate enzyme families, covering 70.5% of all known CAZyme families. A novel multifunctional CAZyme, BfLac15, was identified, which exhibited 24.7% sequence-related similarity. Functional validation confirmed that BfLac15 can degrade both xylan and β-glucan. Conclusions: The constructed large gut microbial CAZyme library expands our knowledge of CAZymes encoded by the animal gut microbiota and provides resources to promote the development and application of CAZymes.
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BibTeX
@article{han2026mining,
title = {{Mining and Characterization of Carbohydrate-Active Enzymes in MAGs from Animal Gut Microbes}},
author = {Lin Han and Ke Tan and Jinming Yu and Wei Ni and Kaiping Liu and Jiangjiao Qi and Shengwei Hu and Xiaoyue Li and Cunyuan Li},
journal = {Molecules},
year = {2026},
month = nov,
doi = {10.3390/molecules31213980},
url = {https://www.mdpi.com/1420-3049/31/21/3980},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Mining and Characterization of Carbohydrate-Active Enzymes in MAGs from Animal Gut Microbes
AU - Lin Han
AU - Ke Tan
AU - Jinming Yu
AU - Wei Ni
AU - Kaiping Liu
AU - Jiangjiao Qi
AU - Shengwei Hu
AU - Xiaoyue Li
AU - Cunyuan Li
PY - 2026
DA - 2026/11/04
JO - Molecules
DO - 10.3390/molecules31213980
UR - https://www.mdpi.com/1420-3049/31/21/3980
AB - Background: CAZymes mediate carbohydrate catabolism in animals and are critical for supporting animal growth, development, metabolism and production performance. This study aimed to explore the gut microbial CAZyme repertoire of humans and multiple animal species and identify novel and efficient CAZymes. Methods: A total of 100,090 MAGs from humans and 10 animal species were collected for CAZyme annotation. PULpy was used to annotates PULs encoded by the Bacteroides. DeepFRI annotation combined with molecular docking was used to screen novel CAZymes. Prokaryotic expression was further performed to obtain the target enzyme and verify its substrate-degrading activity. Results: We annotated 8,747,365 known CAZymes spanning 613 carbohydrate enzyme families, covering 70.5% of all known CAZyme families. A novel multifunctional CAZyme, BfLac15, was identified, which exhibited 24.7% sequence-related similarity. Functional validation confirmed that BfLac15 can degrade both xylan and β-glucan. Conclusions: The constructed large gut microbial CAZyme library expands our knowledge of CAZymes encoded by the animal gut microbiota and provides resources to promote the development and application of CAZymes.
SN - 1420-3049
ER -