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A study on in vitro enzyme inhibitory properties of Asphodeline anatolica: New sources of natural inhibitors for public health problems
Industrial Crops and Products Cilt 83 ss. 39-43
Scopus Toplam 133 atıf DOI
Asphodeline species are traditionally used as food and medicines. The different extracts (acetone, methanol and water) from different parts (stem, root, seed and leaf) of Asphodeline anatolica were screened for inhibitory potentials on cholinesterase, tyrosinase, α-amylase and α-glucosidase. Enzyme inhibitory effects were investigated by using microplate reader. All studied extracts exhibited remarkable inhibitory effects on the tested enzymes. Generally, acetone and methanol extracts have higher potentials than water extracts. Also, the enzyme inhibitory activities of the extracts varied significantly according to the plant parts as well as the solvent used. R-Met (7.42. mgGALAEs/g extract) and St-Ac (10.74. mgGALAEs/g extract) had the highest acetylcholinesterase and butrylcholinesterase inhibitory activity, respectively. R-Met (22.48. mgKAEs/g extract) exhibited the strongest tyrosinase inhibitory effects, while Se-Ac had the most potent activity on both α-amylase (2.53. mmolACAEs/g extract) and α-glucosidase (6.70. mmolACAEs/g extract). The results suggested that the A. anatolica extract may be useful for food and medicinal applications.
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Food-inspired peptides from spinach Rubisco endowed with antioxidant, antinociceptive and anti-inflammatory properties
Food Chemistry X Cilt 18
Scopus Havuzumuzda Open Access 27 atıf almış
Rubiscolin-6 (amino acid sequence: YPLDLF) is a selective δ-opioid receptor peptide isolated from spinach Rubisco. Its synthetic analogue, peptide YPMDIV is the most potent described so far for its increased opioid activity, thus in this work it was considered as lead compound for the design of twelve new analogues e.g. LMAS1-12. Firstly all the novel compounds have been tested for their antinociceptive and anti-inflammatory capacity in vitro and in vivo in order to evaluate their ability to maintain or loss the original activity. Among them peptides LMAS5-8 gave the best results, thus their antioxidant properties have been investigated along with their enzymatic inhibitory ability. Peptide LMAS6 shows a strong antioxidant (154.25 mg TE/g CUPRAC) and inhibitor activity on tyrosinase (84.49 mg KAE/g), indicating a potential role in food industry as anti-browning agent, while peptides LMAS5 and LMAS7 possess a modest cholinesterase inhibitory activity suggesting a conceivable use for nutraceuticals production.
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Kurumlar (6)
HUN-REN Biological Research Centre, Szeged Szeged, Hungary
Istituto Superiore Di Sanita Rome, Italy
NGN Healthcare Torrette, Italy
Selçuk Üniversitesi Selçuklu, Turkey
Università Cattolica del Sacro Cuore, Campus di Roma Rome, Italy
University of G. d'Annunzio Chieti and Pescara Chieti, Italy