Sequence-Structure Based Comparison of Structurally Homologous Thermophilic and Mesophilic Polyethylene Terephthalate (PET) Hydrolases

  • Khomaini Hasan Research Center for Applied Microbiology, National Research and Innovation Agency (BRIN), Jalan Raya Bogor Km. 46, Cibinong, Bogor, Indonesia. Faculty of Medicine, Universitas Jenderal Achmad Yani, Cimahi, Bandung 40525, Indonesia
  • Maria Ulfah Research Center for Applied Microbiology, National Research and Innovation Agency (BRIN), Jalan Raya Bogor Km. 46, Cibinong, Bogor, Indonesia
  • Niknik Nurhayati Research Center for Applied Microbiology, National Research and Innovation Agency (BRIN), Jalan Raya Bogor Km. 46, Cibinong, Bogor, Indonesia
  • Gabriela Christy Sabbathini Research Center for Applied Microbiology, National Research and Innovation Agency (BRIN), Jalan Raya Bogor Km. 46, Cibinong, Bogor, Indonesia
  • Sri Rezeki Wulandari Research Center for Applied Microbiology, National Research and Innovation Agency (BRIN), Jalan Raya Bogor Km. 46, Cibinong, Bogor, Indonesia
  • I Gede Eka Perdana Putra Research Center for Applied Microbiology, National Research and Innovation Agency (BRIN), Jalan Raya Bogor Km. 46, Cibinong, Bogor, Indonesia
  • Is Helianti Research Center for Applied Microbiology, National Research and Innovation Agency (BRIN), Jalan Raya Bogor Km. 46, Cibinong, Bogor, Indonesia

Abstract

Protein structure has a direct impact on thermostability. Deviations in the primary sequence can affect structural changes, leading to alterations in thermostability properties. However, the molecular basis of protein thermostability is unspecified; thus, elucidation of key factors that role particular protein thermostability is required when engineering proteins to be thermostable. To address this challenge, the amino acid composition, hydrophobicity/hydrophilicity ratio, cysteine bridges, and intrinsic features of two structurally homologous but different thermostability, poly(ethylene terephthalate) hydrolase (PETase) were compared. According to the findings, thermostable and thermolabile PETases have similar folds, compactness, and disulfide bridges. Interestingly, an abundance gap of aromaticity, hydrophobic cluster area, polar amino acid and hydrogen bond network compositions demonstrated dominant trends of variations for both PET hydrolases, indicating a pivotal role of these features in the thermostability of PET hydrolase. Furthermore, increased hydrophobic amino acid frequency in the inner surface of thermostable proteins contributed significantly to thermostability by forming more internal hydrophobic interactions and a less hydrophobic patch. There are no consistent trends in insertions and deletions between both PETases. Taken together, these observations demonstrate that hydrophobicity and hydrogen bond networks are essential factors in thermostability of thermostable PETase.

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Published
2023-12-01
How to Cite
HasanK., UlfahM., NurhayatiN., SabbathiniG. C., WulandariS. R., PutraI. G. E. P., & HeliantiI. (2023). Sequence-Structure Based Comparison of Structurally Homologous Thermophilic and Mesophilic Polyethylene Terephthalate (PET) Hydrolases. HAYATI Journal of Biosciences, 31(2), 348-356. https://doi.org/10.4308/hjb.31.2.348-356
Section
Articles