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Novel acid trehalase belonging to glycoside hydrolase family 37 from Pleurotus sp.: cloning, expression and characterization

Summary

Scientists discovered a new enzyme in Pleurotus mushrooms that breaks down trehalose, a special sugar that mushrooms use for growth and survival. This enzyme is unusual because it works in acidic conditions and belongs to a family of enzymes (GH37) that was previously thought only to contain neutral trehalases. The researchers cloned and produced this enzyme in laboratory yeast, then tested its properties to understand how it functions. This discovery helps explain how mushrooms manage their sugar metabolism during growth and decay.

Background

Trehalose is a disaccharide found in fungi that serves as a carbon source and cellular protectant. Two types of trehalases (trehalose-hydrolyzing enzymes) exist: acid and neutral trehalases, classified into glycoside hydrolase families 65 and 37 respectively. However, few reports exist on the structure and function of trehalases in mushrooms.

Objective

To clone, express, and characterize a novel acid trehalase enzyme from Pleurotus sp. that belongs to glycoside hydrolase family 37. The researchers aimed to understand the enzymatic properties and role of this trehalase during fruit-body development and autolysis.

Results

The trehalase gene was 2247 bp encoding 749 amino acids with predicted mass of 81.2 kDa. The recombinant enzyme was approximately 117 kDa with N-glycosylation, optimal pH 4.5 and temperature 40°C. The enzyme showed exclusive activity toward trehalose and was strongly inhibited by validamycin A (IC50 = 0.98 μM).

Conclusion

This is the first report of a novel GH family 37 acid trehalase from Pleurotus sp., representing an unusual classification since acid trehalases typically belong to GH family 65. The enzyme’s biochemical properties and inhibitor sensitivity were characterized, providing insights into trehalose metabolism during mushroom development.
  • Published in:Mycoscience,
  • Study Type:Experimental Research,
  • Source: PMID: 37089524, DOI: 10.47371/mycosci.2022.09.001
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