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. 2012 Feb 2;8(1):4.
doi: 10.1186/2046-9063-8-4.

Function and Biotechnology of Extremophilic Enzymes in Low Water Activity

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Free PMC article

Function and Biotechnology of Extremophilic Enzymes in Low Water Activity

Ram Karan et al. Aquat Biosyst. .
Free PMC article

Abstract

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.

Figures

Figure 1
Figure 1
Distribution of the water molecules near the protein surface predicted from high resolution structures (adapted from ref. 30). The relative number of water molecules versus distance is plotted for a halophilic glucose dehydrogenase enzyme active at low water activity (red) [30] and for non-halophilic enzymes (black). Multiple hydration layers may surround extremophilic proteins as a result of their ability to bind more tightly to water than non-extremophilic proteins.
Figure 2
Figure 2
Distribution of protein isoelectric point in halophilic and non-halophilic organisms predicted from genome sequences (adapted from ref. 13). The percent of all predicted proteins is plotted versus their calculated isoelectric points. The distribution of protein isoelectric points for the halophile Halobacterium sp. NRC-1 (red) is skewed towards acidic range while those of non-halophiles (black) have a broader distribution of isoelectric points with an average of neutrality in most cases.
Figure 3
Figure 3
Structural features of an extremophilic glucose dehydrogenase. The protein structure (PDB ID:2B5V) [30] was downloaded from RCSB Protein Data Bank [123] and illustrated using DeepView Swiss-PdbViewer [124]. (A) Ribbon structure is shown with one subunit colored light gray and one subunit colored dark gray. Boxed region encompassing three α-helices of one subunit and two partial α-helices of the other subunit are shown in detail in part B. Acidic residues (aspartic acid and glutamic acid) are colored red and pink respectively, and basic residues (arginine and lysine) are colored dark blue and medium blue, respectively. Water molecules are colored light purple. (B) Expanded region showing a portion with side chains of exposed acidic residues and buried basic residues. Asterisk indicates residues of the dark gray subunit. An inter-subunit ion pair between Arg289 of one subunit and Asp277 of the other subunit is shown by a line labeled 2.62 Å, the distance between interacting atoms of the two residues.

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