Abstract
Hyperthermophilic Archaea colonizing unnatural habitats of extremes conditions such as volcanoes and deep-sea hydrothermal vents represent an unmeasurable bioresource for enzymes used in various industrial applications. Their enzymes show distinct structural and functional properties and are resistant to extreme conditions of temperature and pressure where their mesophilic homologs fail. In this review, we will outline carbohydrate-active enzymes (CAZymes) from hyperthermophilic Archaea with specific focus on the two largest families, glycoside hydrolases (GHs) and glycosyltransferases (GTs). We will present the latest advances on these enzymes particularly in the light of novel accumulating data from genomics and metagenomics sequencing technologies. We will discuss the contribution of these enzymes from hyperthermophilic Archaea to industrial applications and put the emphasis on newly identifed enzymes. We will highlight their common biochemical and distinct features. Finally, we will overview the areas that remain to be explored to identify novel promising hyperthermozymes.
Highlights
Escherichia coli.rigidity (ii) theythat are (ii) theyproduced are moreand resistant to chemical denaturants, (iii) theyasdisplay higher more resistant to chemical (iii)and they display higher thattemperature is required is required for high protein denaturants, thermostability, they can be used rigidity at a higher for high protein thermostability, they faster can bereaction used at rates a higher temperature whichthercan which can decrease viscosity, (iv)and provide
Glycosyltransferases constitute a large family of carbohydrate-active enzymes (CAZymes) that catalyze the transfer of activated forms of monosaccharides to an appropriate acceptor including lipids, proteins, heterocyclic compounds, or other carbohydrate residues to create a diverse range of valuable glycoconjugates, oligosaccharides and polysaccharides [7,121,122]
The GT5 members are specific to some thermophilic families, the inverting consisting of a GTand using lipid-diphospho-oligosaccharide methanogens such asGT66 the Methanococcales, to hyperthermophilic
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. The database provides online access for the classification follows: the carbohydrate esterases, the polysaccharide lyases, enzymes with auxiliary acof CAZymes into different families based on the similarity of their amino acid sequences, tivities, the the carbohydrate binding modules, the glycosidelyases, hydrolases and with the glycosylas follows: carbohydrate esterases, the polysaccharide enzymes auxiliary transferases. (iii) theyasdisplay higher more resistant to chemical (iii)and they display higher thattemperature is required is required for high protein denaturants, thermostability, they can be used rigidity at a higher for high protein thermostability, they faster can bereaction used at rates a higher temperature whichthercan which can decrease viscosity, (iv)and provide [9,10,11] This enhanced thermostabilmostability is accomplished by the presence of a higher number of hydrophobic amino ity is in accomplished theand presence of a higher number of hydrophobic amino acids in acids the enzyme’sby core an increased number of ionic interactions, surface charges the enzyme’s core and an increased number of ionic interactions, surface charges and and salt bridges
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