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. 2022 Sep 10;23(18):10505.
doi: 10.3390/ijms231810505.

Valorization of Biomasses from Energy Crops for the Discovery of Novel Thermophilic Glycoside Hydrolases through Metagenomic Analysis

Roberta Iacono  1 , Andrea Strazzulli  1   2 , Rosa Giglio  3 , Federica Bitetti  3 , Beatrice Cobucci-Ponzano  3 , Marco Moracci  1   2   3
Affiliations

Valorization of Biomasses from Energy Crops for the Discovery of Novel Thermophilic Glycoside Hydrolases through Metagenomic Analysis

Roberta Iacono et al. Int J Mol Sci. .

Abstract

The increasing interest for environmentally friendly technologies is driving the transition from fossil-based economy to bioeconomy. A key enabler for circular bioeconomy is to valorize renewable biomasses as feedstock to extract high value-added chemicals. Within this transition the discovery and the use of robust biocatalysts to replace toxic chemical catalysts play a significant role as technology drivers. To meet both the demands, we performed microbial enrichments on two energy crops, used as low-cost feed for extremophilic consortia. A culture-dependent approach coupled to metagenomic analysis led to the discovery of more than 300 glycoside hydrolases and to characterize a new α-glucosidase from an unknown hyperthermophilic archaeon. Aglu1 demonstrated to be the most active archaeal GH31 on 4Np-α-Glc and it showed unexpected specificity vs. kojibiose, revealing to be a promising candidate for biotechnological applications such as the liquefaction/saccharification of starch.

Keywords: CAZymes; archaea; enrichments; extremozymes.

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Conflict of interest statement

The authors declare they have no conflict of interest.

Figures

Figure 1
Figure 1
Taxonomic annotation at the genus level.
Figure 2
Figure 2
Distribution of the glycosidases active on axial (a) and equatorial (b) C1-OR bonds.
Figure 3
Figure 3
Close-up superimposition of S. solfataricus MalA C (yellow) and D (orange) domains and Aglu1 model (white).
Figure 4
Figure 4
(a) Dependence of Aglu1 activity on pH. (b) Stability of the Aglu1 activity at pH 4.5. (c) Dependence of Aglu1 activity on temperature. (d) Heat stability of Aglu1.
Figure 5
Figure 5
TLC analysis of the enzymatic assays on maltotriose, maltopentaose and nigerose. Lanes 1 and 9: Glucose. Lane 2: blank on maltotriose. Lane 3: Aglu1 on maltotriose. Lane 4: blank on maltopentaose. Lane 5: Aglu1 on maltopentaose. Lane 6: Maltose. Lane 7: blank on nigerose. Lane 8: Aglu1 on nigerose. G: glucose; M: maltose; G3: maltotriose; G4: maltotetraose; G5: maltopentaose.
Figure 6
Figure 6
Phylogenetic blastx tree of the metagenomic contig containing the gene aglu1 (branch in red).
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