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Two Ganoderma species: Profiling of phenolic compounds by HPLC-DAD, antioxidant, antimicrobial and inhibitory activities on key enzymes linked to diabetes mellitus, Alzheimer's disease and skin disorders
Food and Function Cilt 6 ss. 2794-2802
Scopus Toplam 140 atıf DOI
This work reports the antioxidant, antimicrobial, and inhibitory effects of methanol and water extracts from Ganoderma applanatum (GAM: methanol extract and GAW: water extract) and G. resinaceum (GRM: methanol extract and GRW: water extract) against cholinesterase, tyrosinase, α-amylase and α-glucosidase. The total phenolics, flavonoids contents, and HPLC profile of phenolic components present in the extracts, were also determined. Antioxidant activities were investigated by using different assays, including DPPH, ABTS, FRAP, CUPRAC, phosphomolybdenum and metal chelating assays. Antimicrobial activity of the tested Ganoderma extracts was also studied by the broth microdilution method. Generally, the highest antioxidant (59.24 mg TEs per g extract for DPPH, 41.32 mg TEs per g extract for ABTS, 41.35 mg TEs per g extract for CUPRAC, 49.68 mg TEs per g extract for FRAP, 130.57 mg AAEs per g extract for phosphomolybdenum and 26.92 mg EDTAEs per g extract) and enzyme inhibitory effects (1.47 mg GALAEs per g extract for AChE, 1.51 mg GALAEs per g extract for BChE, 13.40 mg KAEs per g extract for tyrosinase, 1.13 mmol ACEs per g extract for α-amylase and 2.20 mmol ACEs per g extract for α-glucosidase) were observed in GRM, which had the highest concentrations of phenolics (37.32 mg GAEs g-1 extract). Again, Ganoderma extracts possess weak antibacterial and antifungal activities. Apigenin and protocatechuic acid were determined as the main components in GRM (1761 μg per g extract) and GAM (165 μg per g extract), respectively. The results suggest that the Ganoderma species may be considered as a candidate for preparing new food supplements and can represent a good model for the development of new drug formulations.
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Atıf Yapan Yayın
Chemical characterization, antioxidant, enzyme inhibition and antimutagenic properties of eight mushroom species: A comparative study
Journal of Fungi Cilt 6 ss. 1-19
Scopus Havuzumuzda Open Access 45 atıf almış
This study aimed to determine the chemical composition and biologic activities of eight mushroom species (Amanita crocea, Hemileccinum depilatum, Cyclocybe cylindracea, Lactarius deliciosus, Hygrocybe acutoconica, Neoboletus erythropus, Russula aurea and Russula sanguinea). The antioxidant, enzyme inhibitory and mutagenic/antimutagenic activities were evaluated to provide data on the biologic activities. With respect to the chemical composition, LC–MS/MS technique was used to determine individual phenolic compounds present in the extracts. Antioxidant properties were investigated by different chemical methods including radical quenching (DPPH and ABTS), reducing power (CUPRAC and FRAP), phosphomolybdenum and metal chelating. In the enzyme inhibitory assays, cholinesterases, tyrosinase, amylase and glucosidase were used. Mutagenic and antimutagenic properties were evaluated by the Ames assay. In general, the best antioxidant abilities were observed from H. depilatum and N. erythropus, which also showed highest level of phenolics. The best cholinesterase inhibition ability was found from C. cylindracea (1.02 mg GALAE/g for AChE; 0.99 mg GALAE/g for BChE). Tyrosinase inhibition ability varied from 48.83 to 54.18 mg KAE/g. The extracts exhibited no mutagenic effects and showed significant antimutagenic potential. H. acutoconica, in particular depicted excellent antimutagenicity with a ratio of 97% for TA100 and with a rate of 96% for TA98 strain against mutagens in the presence of metabolic activation system. Results presented in this study tend to show that the mushroom species could be exploited as potential sources of therapeutic bioactive agents, geared towards the management of oxidative stress, global health problems and cancer.
Atıf Yapan Makale Bilgileri
Kurumlar (2)
Selçuk Üniversitesi Selçuklu, Turkey
University of Novi Sad Novi Sad, Serbia