Topic Editors

Department of Chemistry, Pukyong National University, Busan 48513, Republic of Korea
Dr. Hackwon Do
Korea Polar Research Institute, Incheon, Republic of Korea

Proteins and Protein-Based Biomaterials from Organisms in Extreme Environments

Abstract submission deadline
30 November 2024
Manuscript submission deadline
31 January 2025
Viewed by
3382

Topic Information

Dear Colleagues,

In the diverse ecosystems of our planet, organisms demonstrate an extraordinary capacity to not only survive but also thrive in the most extreme conditions imaginable. This resilience is not limited to microorganisms, and extends to a wide range of life forms, including plants, invertebrates, and even mammals. These organisms, often referred to as extremophiles, include hyperthermophiles, thermophiles, psychrophiles, acidophiles, basophiles, halophiles, and piezophiles. Each is uniquely adapted to survive in environments ranging from deep sea vents and acidic hot springs to frozen tundras and arid deserts.

The remarkable adaptations of these extremophiles have captivated scientists and led to significant advancements in the life sciences. They have influenced both academic research and society in general. A notable example is the discovery and utilization of Taq DNA polymerase, derived from thermophilic bacteria, and lipases from Candida antarctica, a psychrophilic yeast. Beyond this, the potential of these organisms, particularly in biotechnology, industrial applications, and biomedicine, is vast and largely unexplored. Despite advances in next-generation sequencing and advanced bioinformatics, a significant portion of their proteins remains uninvestigated for practical applications. In addition, the exploration of the protein-based biomaterials derived from these organisms is interesting. A representative example is the ice-binding protein or antifreeze protein. These biomaterials, with their unique properties honed by extreme environments, hold great promise for innovative applications in various fields, including biomedical engineering, environmental remediation, and sustainable material development.

This upcoming Topic, entitled “Proteins and Protein-Based Biomaterials from Organisms in Extreme Environments” aims to delve deeper into this uncharted territory. We seek to encompass a broad spectrum of topics including, but not limited to, the keywords listed below.

Prof. Dr. Hak Jun Kim
Dr. Hackwon Do
Topic Editors

Keywords

  • extremophilic proteins
  • protein design and engineering
  • X-ray crystal structure
  • industrial enzymes
  • antifreeze protein
  • ice-binding protein
  • self-assembly
  • protein-based materials
  • biomaterials

Participating Journals

Journal Name Impact Factor CiteScore Launched Year First Decision (median) APC
Applied Biosciences
applbiosci
- - 2022 34.2 Days CHF 1000 Submit
Applied Sciences
applsci
2.5 5.3 2011 17.8 Days CHF 2400 Submit
Biomolecules
biomolecules
4.8 9.4 2011 16.3 Days CHF 2700 Submit
Materials
materials
3.1 5.8 2008 15.5 Days CHF 2600 Submit
Polymers
polymers
4.7 8.0 2009 14.5 Days CHF 2700 Submit

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Published Papers (2 papers)

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13 pages, 3349 KiB  
Article
Enhancing Paenibacillus sp. Cold-Active Acetyl Xylan Esterase Activity through Semi-Rational Protein Engineering
by Keunho Ji, Sondavid Nandanwar, So Yeon Jeon, Gyu Ri Yang, Lixiao Liu, Hyun-Myung Oh and Hak Jun Kim
Appl. Sci. 2024, 14(13), 5546; https://doi.org/10.3390/app14135546 - 26 Jun 2024
Viewed by 1096
Abstract
Interest in protein engineering for the enzymatic production of valuable products, such as pharmaceutical compounds and biofuels, is growing rapidly. The cold-active acetyl xylan esterase from Paenibacillus sp. (PbAcE) presents unusually broad substrate specificity. Here, we engineered a hydrophobic substrate-binding pocket to enable [...] Read more.
Interest in protein engineering for the enzymatic production of valuable products, such as pharmaceutical compounds and biofuels, is growing rapidly. The cold-active acetyl xylan esterase from Paenibacillus sp. (PbAcE) presents unusually broad substrate specificity. Here, we engineered a hydrophobic substrate-binding pocket to enable the accommodation of relatively large alcohol substrates, such as linalyl acetate and α-terpinyl acetate. To identify candidate residues for engineering, we performed covalent docking of substrates to the Ser185 active site using the HCovDock program. Functional hotspots were analyzed using HotSpot Wizard 3.1. Lys91, His93, and Tyr182 were selected for site-saturation mutagenesis (SSM). After generating the SSM mutant library, a qualitative colorimetric assay was conducted to identify positive mutants. Three, two, and five single mutants were selected for Lys91, His93, and Tyr182, respectively. The best single mutants were then sequentially combined to generate double and triple mutants. Single mutants exhibited a 10–30% increase in activity compared to that of wild-type PbAcE, while no significant synergistic improvements were observed in the double and triple mutants. The increase in activity against both linalyl acetate and α-terpinyl acetate was similar. Mutation did not affect the acetyl binding and catalysis. Further research on the acetyl binding pocket will provide insights into substrate specificity and aid in efficient biocatalyst development for industrial applications. Full article
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18 pages, 3643 KiB  
Article
Cloning, Expression, Characterization and Immobilization of a Recombinant Carboxylesterase from the Halophilic Archaeon, Halobacterium salinarum NCR-1
by Nestor David Ortega-de la Rosa, Evelyn Romero-Borbón, Jorge Alberto Rodríguez, Angeles Camacho-Ruiz and Jesús Córdova
Biomolecules 2024, 14(5), 534; https://doi.org/10.3390/biom14050534 - 30 Apr 2024
Viewed by 1452
Abstract
Only a few halophilic archaea producing carboxylesterases have been reported. The limited research on biocatalytic characteristics of archaeal esterases is primarily due to their very low production in native organisms. A gene encoding carboxylesterase from Halobacterium salinarum NRC-1 was cloned and successfully expressed [...] Read more.
Only a few halophilic archaea producing carboxylesterases have been reported. The limited research on biocatalytic characteristics of archaeal esterases is primarily due to their very low production in native organisms. A gene encoding carboxylesterase from Halobacterium salinarum NRC-1 was cloned and successfully expressed in Haloferax volcanii. The recombinant carboxylesterase (rHsEst) was purified by affinity chromatography with a yield of 81%, and its molecular weight was estimated by SDS-PAGE (33 kDa). The best kinetic parameters of rHsEst were achieved using p-nitrophenyl valerate as substrate (KM = 78 µM, kcat = 0.67 s−1). rHsEst exhibited great stability to most metal ions tested and some solvents (diethyl ether, n-hexane, n-heptane). Purified rHsEst was effectively immobilized using Celite 545. Esterase activities of rHsEst were confirmed by substrate specificity studies. The presence of a serine residue in rHsEst active site was revealed through inhibition with PMSF. The pH for optimal activity of free rHsEst was 8, while for immobilized rHsEst, maximal activity was at a pH range between 8 to 10. Immobilization of rHsEst increased its thermostability, halophilicity and protection against inhibitors such as EDTA, BME and PMSF. Remarkably, immobilized rHsEst was stable and active in NaCl concentrations as high as 5M. These biochemical characteristics of immobilized rHsEst reveal its potential as a biocatalyst for industrial applications. Full article
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