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. 2023 Aug 18;28(16):6120.
doi: 10.3390/molecules28166120.

A New Exopolysaccharide from a Wood-Decaying Fungus Spongipellis borealis for a Wide Range of Biotechnological Applications

Michał Fornal  1 , Monika Osińska-Jaroszuk  2 , Magdalena Jaszek  2 , Dawid Stefaniuk  2 , Adrian Wiater  3 , Iwona Komaniecka  4 , Łukasz Matuszewski  5 , Anna Matuszewska  2
Affiliations

A New Exopolysaccharide from a Wood-Decaying Fungus Spongipellis borealis for a Wide Range of Biotechnological Applications

Michał Fornal et al. Molecules. .

Abstract

Fungi are a unique natural resource rich in polysaccharides, proteins, and other components. Polysaccharides are considered one of the most important bioactive components in fungi. Increasing numbers of studies have confirmed that fungal polysaccharides have various biological activities. Given these facts, the main aim of this investigation was to carry out isolation, identification, and structural characterisation of a new polysaccharide (EPS) derived from laboratory-cultured vegetative mycelium of a new Spongipellis borealis strain isolated from the environment. The examination of monosaccharides in the EPS demonstrated that the isolated biopolymer was composed mainly of glucose, galactose, and mannose monomers. The analysis of the methylation of the studied polymer indicated that it contained mainly terminal, →3)-linked, →4)-linked, and →2,4)-linked hexoses. The effect of fungal polysaccharides on S. borealis proteolytic enzymes (pepsin, trypsin, and pycnoporopepsin) and laccase activity was determined for the first time. Incubation of the enzyme preparation and EPS showed an influence of EPS on the stability of these enzymes, compared to the control values (without EPS).

Keywords: Spongipellis borealis; exopolysaccharide; fungi; laccase; proteolytic enzymes.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Detection of (1→3)-α-D-glucan in the hyphae of S. borealis by means of fluorophore-labelled antibodies (Clone IgM MOPC-104E). (A) Filaments in light microscopy, (B) fluorescent image of the same filaments. Twenty samples were observed, and typical images are presented. Scale bar = 50 µm.
Figure 2
Figure 2
FT-IR spectrum of polysaccharides (EPS) obtained from S. borealis.
Figure 3
Figure 3
FT-IR spectrum of polysaccharides (EPS) obtained from S. borealis—after deproteination.
Figure 4
Figure 4
Proteolytic enzyme activity with or without EPS from S. borealis. The experiments were performed in triplicate. Average relative values (n = 3) and error bars are shown. Values with p ≤ 0.05 are significantly different (** p ≤ 0.01; *** p ≤ 0.001).
Figure 5
Figure 5
Effect of temperature on laccase stability without (control (A)) or with (B) EPS from S. borealis. The experiments were performed in triplicate. Average relative values (n = 3) and error bars are shown.
Figure 6
Figure 6
Effect of pH on laccase stability without (control) or with EPS from S. borealis. The experiments were performed in triplicate. Average relative values (n = 3) and error bars are shown.
Figure 7
Figure 7
Laccase stability in the presence of surfactants and with or without EPS from S. borealis. The experiments were performed in triplicate. Average relative values (n = 3) and error bars are shown. Values with p ≤ 0.05 are significantly different (*** p ≤ 0.001).
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