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A Novel Hydrophobin Encoded by HGFII from Grifola frondosa Exhibiting Excellent Self-Assembly Ability

Summary

Scientists have discovered a new protein from the mushroom Grifola frondosa that has unique self-assembling properties. This protein, called HGFII, can naturally organize itself into tiny structures and make surfaces water-repellent. It’s also very good at mixing oil and water together stably. Impacts on everyday life: – Could lead to better food preservatives and emulsifiers for processed foods – May help develop new drug delivery systems that are more effective – Could be used to create water-resistant coatings for various materials – Potential applications in creating more environmentally friendly packaging materials – May help develop new antimicrobial surfaces for medical devices

Background

Hydrophobins are small proteins from filamentous fungi that have remarkable self-assembly properties with potential applications as drug carriers and anti-bacterial agents. HGFI, a previously known class I hydrophobin from Grifola frondosa, can self-assemble into rodlet structures 100-150nm in length. New hydrophobins with improved properties are needed for expanded applications.

Objective

To identify and characterize a new hydrophobin gene (hgfII) from the mycelium of G. frondosa and compare its properties to the known HGFI hydrophobin.

Results

HGFII showed much higher transcriptional levels than hgfI in mycelium. The protein successfully self-assembled into rodlet-like structures 15-30nm in diameter, confirming it as a class I hydrophobin but with different assembly behavior than HGFI. HGFII demonstrated stronger surface hydrophobicity than HGFI and displayed superior dispersive capacity with soybean oil, producing more stable and durable emulsions.

Conclusion

HGFII represents a novel class I hydrophobin from G. frondosa with distinct properties from the previously known HGFI. It exhibits excellent self-assembly abilities, forming shorter rodlet structures, stronger surface hydrophobicity, and better emulsification properties than HGFI. These differences make HGFII promising for expanding practical applications of class I hydrophobins.
  • Published in:Frontiers in Microbiology,
  • Study Type:Laboratory Research,
  • Source: 10.3389/fmicb.2022.990231
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