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Function and biotechnology of extremophilic enzymes in low water activity
Open accessAbstract
Enzymes from extremophilic microorganisms usually catalyze chemical reactions in non-standard conditions. Such conditions promote aggregation, precipitation, and denaturation, reducing the activity of most non-extremophilic enzymes, frequently due to the absence of sufficient hydration. Some extremophilic enzymes maintain a tight hydration shell and remain active in solution even when liquid water is limiting, e.g. in the presence of high ionic concentrations, or at cold temperature when water is close to the freezing point. Extremophilic enzymes are able to compete for hydration via alterations especially to their surface through greater surface charges and increased molecular motion. These properties have enabled some extremophilic enzymes to function in the presence of non-aqueous organic solvents, with potential for design of useful catalysts. In this review, we summarize the current state of knowledge of extremophilic enzymes functioning in high salinity and cold temperatures, focusing on their strategy for function at low water activity. We discuss how the understanding of extremophilic enzyme function is leading to the design of a new generation of enzyme catalysts and their applications to biotechnology.
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Cites
From Water and Ions to Crowded Biomacromolecules: In Vivo Structuring of a Prokaryotic Cell
Spitzer, J. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00010-11 · Cited by 77
Metal binding and activation of the ribonuclease H domain from moloney murine leukemia virus
Goedken, E. R., & Marqusee, S. (1999) · Protein Engineering, Design and Selection · doi:10.1093/protein/12.11.975 · Cited by 14
Cited by
Strategies for Stabilization of Enzymes in Organic Solvents
Stepankova, V., Bidmanova, S., Koudelakova, T., Prokop, Z., Chaloupkova, R., & Damborsky, J. (2013) · ACS Catalysis · doi:10.1021/cs400684x · Cited by 659
Upgrading Laccase Production and Biochemical Properties: Strategies and Challenges
Bertrand, B., Martínez‐Morales, F., & Trejo‐Hernández, M. R. (2017) · Biotechnology Progress · doi:10.1002/btpr.2482 · Cited by 62
Metadata
- Authors
- Karan, R., Capes, M. D., & DasSarma, S.
- Venue
- Aquatic Biosystems
- Published
- 2012-02-02
- Volume
- 8
- Issue
- 1
- Pages
- 4-4
- ISSN
- 2046-9063 (ISSN-L)
- OpenAlex
- W2135989046
- Cited by
- 260
- References
- 2
- FWCI
- 5.00
- Type
- journal article
- Language
- en
- Open access
- hybrid
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