Characterization of a GDS(L)-like Hydrolase from Pleurotus sapidus with an Unusual SGNH Motif
- Author: mycolabadmin
- 2024-09-03
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Summary
This research characterized a new type of enzyme from oyster mushroom that could help break down plant materials more efficiently. The enzyme has unique structural features that make it different from similar known enzymes, suggesting it might represent a new class of biomass-degrading proteins. Impact on everyday life:
– Could lead to more efficient processing of plant waste into useful products
– May help develop more environmentally friendly industrial processes
– Could contribute to reducing dependence on fossil fuels through better biomass utilization
– Potential applications in detergent and cleaning products due to stability in alkaline conditions
– May help improve production of biofuels and bio-based materials
Background
GDSL hydrolases are important enzymes for biomass degradation and contain characteristic amino acid motifs. However, fungal GDSL enzymes, particularly from Basidiomycota, are underrepresented in databases and their functions are often unclear. Understanding these enzymes is crucial for efficient biomass conversion and sustainable development.
Objective
To characterize a novel GDS(L)-like hydrolase (PSA_Lip) from the basidiomycete Pleurotus sapidus through heterologous expression, biochemical characterization, and structural analysis. The study aimed to understand its unique structural features and potential functions.
Results
PSA_Lip was successfully expressed with an activity of 350 U L−1. The enzyme showed optimal activity at pH 8 and 65°C, with high stability at pH 10. Unlike typical GDSL hydrolases, PSA_Lip contained an unusual SGGI motif instead of the conventional SGNH motif. The enzyme showed highest activity towards medium chain-length p-nitrophenyl octanoate, with limited activity towards other substrates.
Conclusion
PSA_Lip represents a novel type of GDS(L)-like hydrolase with unique structural features, particularly its unusual SGGI motif. The enzyme’s distinct characteristics suggest it may represent a new class of carbohydrate esterases, with potential applications in alkaline conditions due to its pH stability.
- Published in:AMB Express,
- Study Type:Experimental Research,
- Source: 10.1186/s13568-024-01752-x