Pressurized Liquid (PLE) Truffle Extracts Have Inhibitory Activity on Key Enzymes Related to Type 2 Diabetes (α-Glucosidase and α-Amylase)

Autor: Tejedor Calvo, Eva, Morales, Diego, Morillo, Laura, Vega, Laura, Caro, Mercedes, Ribeiro Smiderle, Fhernanda, Iacomini, Marcello, Marco Montori, Pedro, Soler Rivas, Cristina
Jazyk: angličtina
Rok vydání: 2023
Předmět:
Popis: An optimized PLE method was applied to several truffle species using three different solvent mixtures to obtain bioactive enriched fractions. The pressurized water extracts contained mainly (1 ? 3),(1 ? 6)-?-D-glucans, chitins, and heteropolymers with galactose and mannose in their structures. The ethanol extracts included fatty acids and fungal sterols and others such as brassicasterol and stigmasterol, depending on the species. They also showed a different fatty acid lipid profile depending on the solvent utilized and species considered. Ethanol:water extracts showed interesting lipids and many phenolic compounds; however, no synergic extraction of compounds was noticed. Some of the truffle extracts were able to inhibit enzymes related to type 2 diabetes; pressurized water extracts mainly inhibited the ?-amylase enzyme, while ethanolic extracts were more able to inhibit ?-glucosidase. Tuber brumale var. moschatum and T. aestivum var. uncinatum extracts showed an IC50 of 29.22 mg/mL towards ?-amylase and 7.93 mg/mL towards ?-glucosidase. Thus, use of the PLE method allows o bioactive enriched fractions to be obtained from truffles with antidiabetic properties. This research was funded by the fellowship Ibercaja-CAI Estancias de Investigación number CA 1/20. The research leading to these results has received funding from the European Union under “Horizon 2020—the Framework Programme for Research and Innovation (2014–2020)”. Grant Agreement of the Project: “Innovation in truffle cultivation, preservation, processing and wild truffle resources management”, INTACT, Project number 101007623. truffles β-D-glucans ergosterol fatty acids antidiabetic amylase glucosidase Published
Databáze: OpenAIRE