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Engineering of β-Agarase with Enhanced Thermostability via Multitool Consensus Prediction and Structure-Guided

Qianqian Diao1,2,3, Xingfei Li1,2,3, Yuxiang Bai1,2

  • 1The State Key Laboratory of Food Science and Resources, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.

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Engineered beta-agarase (β-Agarase) shows enhanced thermostability for producing valuable agar oligosaccharides. This breakthrough improves enzyme applications in high-temperature industrial processes.

Keywords:
molecular dynamics simulationrational designthermostabilityβ-agarase

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Area of Science:

  • Biotechnology
  • Enzyme Engineering
  • Biochemistry

Background:

  • β-Agarase is essential for producing bioactive agar oligosaccharides.
  • Limited thermostability of wild-type β-Agarase hinders industrial applications.
  • Developing thermostable β-Agarase is crucial for efficient industrial production.

Purpose of the Study:

  • To enhance the thermostability of β-Agarase (AgaDcat) for industrial applications.
  • To develop an efficient enzyme engineering strategy for improving thermostability.
  • To investigate the structural basis for enhanced thermostability.

Main Methods:

  • A stepwise design strategy combining consensus prediction, structure-based screening, and greedy optimization.
  • Site-directed mutagenesis to create the M3 variant (N120S-D243N-Q246A-S287E-A335D).
  • Molecular dynamics simulations to analyze structural changes and interaction networks.

Main Results:

  • Mutant M3 exhibited an 11 °C higher melting temperature and a 14-fold longer half-life at 50 °C compared to wild-type.
  • Molecular dynamics revealed strengthened hydrophobic interactions, salt bridges, and hydrogen bonding in M3.
  • The M3 variant efficiently hydrolyzed agarose at high temperatures, producing neoagarotetraose (NA4) and neoagarohexaose (NA6).

Conclusions:

  • The engineered M3 β-Agarase demonstrates significantly improved thermostability and industrial potential.
  • The applied stepwise enzyme engineering framework enhances efficiency for industrial enzyme modification.
  • This approach offers a general strategy for improving the thermostability of industrial enzymes.