Natural methods of protein stabilization: thermostable biocatalysts

Abstract

Enzymes that are naturally found in thermophilic and hyperthermophilic organisms are being used as robust biocatalysts in the fine chemical and pharmaceutical industries. They have important use in these industries due to their increased stability which is often required during commercial reaction conditions. The approach used in these studies is to learn how nature has managed to stabilize these proteins using a detailed knowledge of their biochemical properties and three-dimensional structures. This is illustrated with several different classes of enzyme that have been studied at Exeter. These include alcohol dehydrogenase, aminoacylase, pyroglutamyl carboxypeptidase, gamma-lactamase, dehalogenase and lysophospholipase.

Evaluation of a novel Bacillus strain from a north‐western Spain hot spring as a source of extracellular thermostable lipase

“…Additionally, their study could provide useful information concerning the structure-function relationships in catalytic proteins. 4,5 However, much work remains to be done on this topic. The number of known thermophilic microorganisms is limited, and very often their most interesting enzymes are intracellular or membrane-bound.…”

Assessment of Relevant Factors Influencing Lipolytic Enzyme Production by Thermus thermophilus HB27 in Laboratory‐Scale Bioreactors

“…In fact, proteins from these organisms show more resistance to high temperatures, proteolysis, and chemical denaturation. By being able to work at higher temperatures, these enzymes could offer an advantage, since in this case the solubility and diffusion rate of reactants would be higher and the medium viscosity would be lower [1].…”

“…The typical natural substrates of lipases are long-chain triacylglycerides, while esterases are usually considered to catalyze reactions involving short-chain fatty acids [2]. Thermophilic enzymes with lipolytic activity would allow operation at higher temperatures, increasing reaction rate and solubility, and decreasing the need of using organic solvents [1,3,4].…”

Discovery and characterization of thermophilic limonene‐1,2‐epoxide hydrolases from hot spring metagenomic libraries

“…the direct extraction and cloning of DNA from natural environments without culturing isolated microorganisms to discover novel enzymes, has been widely demonstrated in recent years [19][20][21][22]. Thermostable hydrolases with different activities, such as lipases, proteases and glycosidases, have already been identified from (hyper)thermophiles [23,24]; however, there is still no evidence for naturally thermostable EHs or the occurrence of this enzymatic activity in hot environments.…”