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  • Title: HPLC-FRAP methodology and biological activities of different stem bark extracts of Cajanus cajan (L.) Millsp.
    Author: Sinan KI, Mahomoodally MF, Eyupoglu OE, Etienne OK, Sadeer NB, Ak G, Behl T, Zengin G.
    Journal: J Pharm Biomed Anal; 2021 Jan 05; 192():113678. PubMed ID: 33120308.
    Abstract:
    Cajanus cajan. (L.) Millsp. (C. cajan) (Family: Fabaceae) also known as pigeon pea, is a famous food and cover/forage crop bearing a high amount of key amino acids (methionine, lysine and tryptophan). This study investigated into the total phenolic (TPC), flavonoid content (TFC), antioxidant [2,2-diphenyl-1-picrylhydrazyl (DPPH), 2,2 -azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), ferric reducing antioxidant power (FRAP), cupric reducing antioxidant capacity, total antioxidant capacity (TAC) (phosphomolybdenum) and metal chelating] activities and enzyme [α-amylase, α-glucosidase, tyrosinase, acetyl-(AChE), butyryl-(BChE) cholinesterase] inhibitory effects of four extracts (methanol, hexane, ethyl acetate, aqueous) prepared from C. cajan stem bark. Direct identification of antioxidants was also conducted using the high performance liquid chromatography-ferric reducing antioxidant power (HPLC-FRAP) system. The highest TPC and TFC were recorded with the methanolic (23.22 ± 0.17 mg GAE/g) and ethyl acetate extracts (19.43 ± 0.24 mg RE/g), respectively. The methanolic extract exhibited important antioxidant activity with DPPH (38.41 ± 0.05 mg Trolox equivalent (TE)/g), ABTS (70.49 ± 3.62 mg TE/g), CUPRAC (81.86 ± 2.40 mg TE/g), FRAP (42.96 ± 0.59 mg TE/g) and metal chelating (17.00 ± 1.26 mg ethylenediaminetetraacetic acid equivalent/g). p-coumaric and caffeic acid were the predominant antioxidants in the samples. Results from enzymatic assays showed the potential abilities of hexane extract in inhibiting the AChE, BChE, α-amylase and α-glucosidase enzymes. From the results obtained in this study, it can be concluded that C. cajan can be considered as a promising source of antioxidants and key enzyme inhibitors that can be exploited for future bioproduct development.
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