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Extremozymes for Industrial Biocatalysis and Green Chemistry

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: 20 March 2025 | Viewed by 1726

Special Issue Editor


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Guest Editor
1. Facultad de Química y Biología, Universidad de Santiago de Chile, Alameda 3363, Santiago 9170022, Chile
2. Fundación Científica y Cultural Biociencia, José Domingo Cañas 2280, Ñuñoa, Santiago 7750132, Chile
Interests: extremophiles; extremozymes; biotechnology; astrobiology

Special Issue Information

Dear Colleagues,

Biocatalysis has proven to be an essential industrial tool for converting raw material into valuable bio-products. The discovery of new enzymes, the improvement of enzymatic features and the development of new processes for enzyme production will drive future innovation.

For the chemical industry, the use of enzymes presents important benefits, which include higher selectivity, increased sustainability and a low toxicity. These efforts in novel green chemistry processes are translated to cleaner production and lower environmental impact at the industrial and global levels.

Enzymes derived from extremophiles, or extremozymes, have already adapted to thrive in environments that present extreme physicochemical conditions. They often have natural outstanding properties, which include being able to carry out reactions under nonstandard conditions (e.g., high or low temperatures, acidic or alkaline pH, high concentrations of salt or organic solvents, and high pressure) where traditional mesophilic enzymes underperform. Moreover, extremozymes are a better starting point for protein design and engineering.

This Special Issue aims to present recent advances in the discovery of novel enzymes derived from extremophiles, their use to design or optimize biotechnological processes and/or potential industrial applications.

We invite researchers to contribute original articles, as well as reviews regarding the isolation and characterization of different types of extremozymes in their native and recombinant versions (including engineered proteins), which could contribute to improve the current knowledge for future developments of novel industrial biocatalysts.

This Special Issue is supervised by Dr. Jenny Blamey and assisted by our Topical Advisory Panel Member Dr. Giannina Espina (Fundación Científica y Cultural Biociencia).

Dr. Jenny M. Blamey
Guest Editor

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Keywords

  • extremophiles
  • extremozymes
  • industrial biocatalysis
  • biotechnology

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Published Papers (1 paper)

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Research

15 pages, 1747 KiB  
Article
Recombinant Expression and Characterization of a Novel Thermo-Alkaline Lipase with Increased Solvent Stability from the Antarctic Thermophilic Bacterium Geobacillus sp. ID17
by Diego Salas-Bruggink, Hardy Guzmán, Giannina Espina and Jenny M. Blamey
Int. J. Mol. Sci. 2024, 25(14), 7928; https://doi.org/10.3390/ijms25147928 - 19 Jul 2024
Viewed by 1210
Abstract
Lipases are enzymes that hydrolyze long-chain carboxylic esters, and in the presence of organic solvents, they catalyze organic synthesis reactions. However, the use of solvents in these processes often results in enzyme denaturation, leading to a reduction in enzymatic activity. Consequently, there is [...] Read more.
Lipases are enzymes that hydrolyze long-chain carboxylic esters, and in the presence of organic solvents, they catalyze organic synthesis reactions. However, the use of solvents in these processes often results in enzyme denaturation, leading to a reduction in enzymatic activity. Consequently, there is significant interest in identifying new lipases that are resistant to denaturing conditions, with extremozymes emerging as promising candidates for this purpose. Lip7, a lipase from Geobacillus sp. ID17, a thermophilic microorganism isolated from Deception Island, Antarctica, was recombinantly expressed in E. coli C41 (DE3) in functional soluble form. Its purification was achieved with 96% purity and 23% yield. Enzymatic characterization revealed Lip7 to be a thermo-alkaline enzyme, reaching a maximum rate of 3350 U mg−1 at 50 °C and pH 11.0, using p-nitrophenyl laurate substrate. Notably, its kinetics displayed a sigmoidal behavior, with a higher kinetic efficiency (kcat/Km) for substrates of 12-carbon atom chain. In terms of thermal stability, Lip7 demonstrates stability up to 60 °C at pH 8.0 and up to 50 °C at pH 11.0. Remarkably, it showed high stability in the presence of organic solvents, and under certain conditions even exhibited enzymatic activation, reaching up to 2.5-fold and 1.35-fold after incubation in 50% v/v ethanol and 70% v/v isopropanol, respectively. Lip7 represents one of the first lipases from the bacterial subfamily I.5 and genus Geobacillus with activity and stability at pH 11.0. Its compatibility with organic solvents makes it a compelling candidate for future research in biocatalysis and various biotechnological applications. Full article
(This article belongs to the Special Issue Extremozymes for Industrial Biocatalysis and Green Chemistry)
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