Abstract
Cold-active enzymes have recently gained popularity because of their high activity at lower temperatures than their mesophilic and thermophilic counterparts, enabling them to withstand harsh reaction conditions and enhance industrial processes. Cold-active lipases are enzymes produced by psychrophiles that live and thrive in extremely cold conditions. Cold-active lipase applications are now growing in the detergency, synthesis of fine chemicals, food processing, bioremediation, and pharmaceutical industries. The cold adaptation mechanisms exhibited by these enzymes are yet to be fully understood. Using phylogenetic analysis, and advanced deep learning-based protein structure prediction tool Alphafold2, we identified an evolutionary processes in which a conserved cold-active-like motif is presence in a distinct subclade of the tree and further predicted and simulated the three-dimensional structure of a putative cold-active lipase with the cold active motif, Glalip03, from Glaciozyma antarctica PI12. Molecular dynamics at low temperatures have revealed global stability over a wide range of temperatures, flexibility, and the ability to cope with changes in water and solvent entropy. Therefore, the knowledge we uncover here will be crucial for future research into how these low-temperature-adapted enzymes maintain their overall flexibility and function at lower temperatures.
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Data Availability
The input files and datasets supporting this study’s findings are available on Zenodo. https://doi.org/https://doi.org/10.5281/zenodo.8323196
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The authors would also like to thank the Universiti Putra Malaysia for their GP-IPB grant (vote number: 9708100) and TETFUND Nigeria for providing a scholarship to the first author.
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GP-IPB Universiti Putra Malaysia supported this project under Grant Number: 9708100.
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Matinja, A.I., Kamarudin, N.H.A., Leow, A.T.C. et al. Structural Insights into Cold-Active Lipase from Glaciozyma antarctica PI12: Alphafold2 Prediction and Molecular Dynamics Simulation. J Mol Evol (2024). https://doi.org/10.1007/s00239-024-10219-3
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DOI: https://doi.org/10.1007/s00239-024-10219-3