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Food and Function 2019-Aug

Phoenix dactylifera L. seeds: a by-product as a source of bioactive compounds with antioxidant and enzyme inhibitory properties.

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Ouarda Djaoudene
Víctor López
Guillermo Cásedas
Francisco Les
Connie Schisano
Mostapha Bey
Gian Tenore

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Date (Phoenix dactylifera L.) seeds are a valuable and abundant by-product with various potential food applications and a source of functional and bioactive ingredients. In this study, date seeds from eight cultivars (Ourous "OUR", Tazizaout "TAZ", Tazarzeit "TAR", Tazoughart "TAG", Ouaouchet "OUC", Oukasaba "OUK", Delat "DEL" and Tamezwertn'telet "TWT") cultivated in the M'zab oasis (south of Algeria) were analyzed for their chemical and phytochemical compositions, antioxidant capacities and in vitro inhibition of some enzymes. Variations in chemical compositions were observed in the studied date seeds. The greatest contents of total phenolic compounds (476 mg GAE per g dw), total flavonoids (6.52 mg QE per g dw), anthocyanins (1.26 mg Q3GE per g dw), flavonols (3.36 mg Q3GE per g dw), proanthocyanidins (85.13 mg CE per g dw), and ascorbic acid were detected in the seeds of the TAG cultivar. All extracts manifested good antioxidant activities tested by ORAC and FRAP assays. The OUC and OUR extracts displayed the most potent antioxidant capacity against DPPH˙ free radicals (IC50 = 37.30 μg ml-1) and ABTS˙+ cation radicals (IC50 = 13.89 μg ml-1), respectively. The antioxidant activity evaluated through a xanthine/xanthine oxidase system demonstrated that the TAZ extract was more efficient as a superoxide radical scavenger (IC50 = 9.08 μg ml-1). Date seed extracts (DSE) exhibited inhibitory activities on enzymes, showing substantial potential as skin-whitening, neuroprotective, anti-hyperglycemic or anti-hyperlipidemic agents; the inhibitory potential was tested using tyrosinase (TYR), acetylcholinesterase (AChE), α-glucosidase (α-GLU) and lipase. All date seed cultivars were able to inhibit tyrosinase and α-glucosidase in a dose-dependent manner reaching the maximum inhibition.

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