An individual alginate lyase is effective in the disruption of Laminaria digitata recalcitrant cell wall

In the present study, 199 pre-selected Carbohydrate-Active enZymes (CAZymes) and sulfatases were assessed, either alone or in combination, to evaluate their capacity to disrupt Laminaria digitata cell wall, with the consequent release of interesting nutritional compounds. A previously characterized individual alginate lyase, belonging to the family 7 of polysaccharide lyases (PL7) and produced by Saccharophagus degradans, was shown to be the most efcient in the in vitro degradation of L. digitata cell wall. The alginate lyase treatment, compared to the control, released up to 7.11 g/L of reducing sugars (p< 0.001) and 8.59 mmol/100 g dried alga of monosaccharides (p< 0.001), and reduced cell wall fuorescence intensity by 39.1% after staining with Calcofuor White (p= 0.001). The hydrolysis of gel-forming polymer alginate by the alginate lyase treatment could prevent the trapping of fatty acids and release benefcial monounsaturated fatty acids, particularly 18:1c9 (p < 0.001), to the extracellular medium. However, no liberation of proteins (p > 0.170) or pigments (p > 0.070) was observed. Overall, these results show the ability of an individual alginate lyase, from PL7 family, to partially degrade L. digitata cell wall under physiological conditions. Therefore, this CAZyme can potentially improve the bioavailability of L. digitata bioactive compounds for monogastric diets, with further application in feed industry.

Description

Research Areas: Science & Technology - Other Topics

Keywords

Fatty-acid profiles Barley-based diets Extracellular-matrix Chlorella-vulgaris Phenolic-compounds Nutritive-value Brown Extraction Algae Fucoxanthin

URI

http://hdl.handle.net/10400.5/22535

Citation

Costa M, Pio L, Bule P, Cardoso V, Alfaia CM, Coelho D, Bras J, Fontes CMGA, Prates JAM. 2021. An individual alginate lyase is effective in the disruption of Laminaria digitata recalcitrant cell wall. Scientific Reports, 11(1):9706. DOI:10.1038/s41598-021-89278-1