Biomass-degrading glycoside hydrolases of archaeal origin

Abstract

During the last decades, the impact of hyperthermophiles and their enzymes has been intensively investigated for implementation in various high-temperature biotechnological processes. Biocatalysts of hyperthermophiles have proven to show extremely high thermo-activities and thermo-stabilities and are identified as suitable candidates for numerous industrial processes with harsh conditions, including the process of an efficient plant biomass pretreatment and conversion. Already-characterized archaea-originated glycoside hydrolases (GHs) have shown highly impressive features and numerous enzyme characterizations indicated that these biocatalysts show maximum activities at a higher temperature range compared to bacterial ones. However, compared to bacterial biomass-degrading enzymes, the number of characterized archaeal ones remains low. To discover new promising archaeal GH candidates, it is necessary to study in detail the microbiology and enzymology of extremely high-temperature habitats, ranging from terrestrial to marine hydrothermal systems. State-of-the art technologies such as sequencing of genomes and metagenomes and automated binning of genomes out of metagenomes, combined with classical microbiological culture-dependent approaches, have been successfully performed to detect novel promising biomass-degrading hyperthermozymes. In this review, we will focus on the detection, characterization and similarities of archaeal GHs and their unique characteristics. The potential of hyperthermozymes and their impact on high-temperature industrial applications have not yet been exhausted.

Activity and stability of hyperthermostable cellulases and xylanases in ionic liquids

“…Several reports have demonstrated the benefit of using hyperthermostable glycoside hydrolases in the hydrolysis of lignocelluloses compared to less thermostable enzymes (Peng et al 2015;H€ am€ al€ ainen et al 2016;Benedetti et al 2019;Han, Yang, et al 2020). In addition to hyperthermostable glycoside hydrolases found in thermophilic and hyperthermophilic microorganisms (Khare et al 2015;Shuddhodana et al 2018, Suleiman et al 2020) many such enzymes have also been found in metagenomic sources (Mientus et al 2013;Gladden et al 2014;Escuder-Rodr ıguez et al 2018). High thermostability appears to protect against denaturation by hydrophilic ILs.…”

Xyloglucan Oligosaccharides Hydrolysis by Exo-Acting Glycoside Hydrolases from Hyperthermophilic Microorganism Saccharolobus solfataricus

“…In particular, hyperstable carbohydrate active enzymes (cazymes) from (hyper)thermophilic archaea show maximum activity at higher temperature ranges compared to mesophilic cazymes. However, archaeal GHs are poorly represented in CAZy and less studied compared to their bacterial counterparts [ 5 ]. Moreover, although most of the GHs annotated in the CAZy database have been characterized by using synthetic substrates, in the framework of biomass saccharification, it is important to test their activity on natural substrates and, more importantly, to investigate their synergistic action on this type of substrate.…”

The Diversity, Composition, and Metabolic Pathways of Archaea in Pigs

“…In general, bacteria in the mammal gut, especially species belonging to Firmicutes and Bacteroidetes, were considered the main providers of CA-Zyme genes for encoding enzymes to digest complex carbohydrates [44]. Nevertheless, recent publications revealed that archaea participate in carbohydrate metabolism through the production of various enzymes [45,46]. In our study, 297 CAZyme gene families were detected in archaea reads, and six of the top 10 CAZyme families of archaea and bacteria were shared.…”