Back to Search Start Over

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

Authors :
Luís Pio
José A. M. Prates
Vânia Cardoso
Diogo Coelho
Joana L. A. Brás
Cristina M. Alfaia
Pedro Bule
Mónica Costa
Carlos M. G. A. Fontes
Source :
Repositório Científico de Acesso Aberto de Portugal, Repositório Científico de Acesso Aberto de Portugal (RCAAP), instacron:RCAAP, Scientific Reports, Scientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
Publication Year :
2021
Publisher :
Nature Research, 2021.

Abstract

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 efficient 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 p p = 0.001). The hydrolysis of gel-forming polymer alginate by the alginate lyase treatment could prevent the trapping of fatty acids and release beneficial monounsaturated fatty acids, particularly 18:1c9 (p 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.

Details

Language :
English
Database :
OpenAIRE
Journal :
Repositório Científico de Acesso Aberto de Portugal, Repositório Científico de Acesso Aberto de Portugal (RCAAP), instacron:RCAAP, Scientific Reports, Scientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
Accession number :
edsair.doi.dedup.....17a6ee641604b9e8f7f74582b739d6ab