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Uncovering the β-1,6-galactan-degrading machinery: Biochemical and functional insights into a processive
Shreya Biswas1, Gurleen Kaur Bagga1, Parmeshwar Vitthal Gavande1
1Carbohydrate Enzyme Biotechnology Laboratory, Department of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Guwahati, Assam, India.
Carbohydrate Research
|December 14, 2025
Summary
This study identifies RfGH30 from Ruminococcus flavefaciens as a novel processive exo-β-1,6-galactanase, crucial for breaking down plant arabinogalactans in the rumen. Its unique activity offers potential for biomass valorization.
Area of Science:
- Biochemistry
- Enzymology
- Microbiology
Background:
- Glycoside hydrolase family 30 (GH30) enzymes are crucial for carbohydrate metabolism.
- Ruminococcus flavefaciens is a key bacterium in ruminal digestion of plant polysaccharides.
Purpose of the Study:
- To biochemically characterize the GH30 enzyme RfGH30 from Ruminococcus flavefaciens.
- To determine its substrate specificity, catalytic properties, and potential applications.
Main Methods:
- Enzyme purification and zymogram analysis.
- Substrate specificity assays using natural and synthetic substrates.
- Kinetic analysis, pH and temperature stability tests.
- Product profile analysis using TLC, HPLC, and HRMS.
Main Results:
- RfGH30 functions as a processive exo-β-1,6-galactanase, not an endoxylanase.
- Optimal activity at pH 5.5 and 40°C, with broad stability.
- High specific activity against larchwood arabinogalactan (LWAG) and sugarbeet arabinan.
- Predominant release of β-1,6-galactobiose from LWAG, indicating strict linkage cleavage.
- High processivity index (21) for LWAG.
Conclusions:
- RfGH30 is the first characterized GH30 processive exo-β-1,6-galactanase from R. flavefaciens.
- Provides insights into ruminal degradation of plant arabinogalactans.
- Demonstrates potential for biomass valorization applications.
