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<p>Yellow turmeric (YT) <i>Curcuma longa</i> L., is a terpenoid derivative with therapeutic prospects. The molecular interaction of its methanolic extract with the&#xa0;diabetic linked enzyme, α-glucosidase was investigated using multi-spectroscopic approaches under simulated physiological intestinal conditions. Antidiabetic activities of YT were assessed by α-glucosidase inhibition assay and its antioxidant capacities are examined by DPPH and ABTS assay. The results indicated that YT quenches the intrinsic fluorescence of α-glucosidase following a mixed quenching mechanism accompanied by a&#xa0;hydrophobic (ΔS° &gt; 0 and ΔH° &gt; 0), endothermic, spontaneous and entropy-driven process that was mainly Tryptophan gated. The enzyme's structural conformation was compromised, as revealed by synchronous and UV-absorption spectroscopy. The extract showed more potent inhibition against α-glucosidase with an&#xa0;IC<sub>50</sub> value of 153&#xa0;µg/mL and relatively DPPH and ABTS scavenging activity. This study provides preliminary data for the plant's potential use in the management of hyperglycemia and α-glucosidase implicated pathological conditions.</p>

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Spectroscopic and antioxidant dependency of natural food dye (yellow turmeric) and its molecular interaction with α-glucosidase

  • 期刊论文

  • 发表日期：

    2025年3月7日

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  • Adejoke N. Kolawole

摘要

Yellow turmeric (YT) Curcuma longa L., is a terpenoid derivative with therapeutic prospects. The molecular interaction of its methanolic extract with the diabetic linked enzyme, α-glucosidase was investigated using multi-spectroscopic approaches under simulated physiological intestinal conditions. Antidiabetic activities of YT were assessed by α-glucosidase inhibition assay and its antioxidant capacities are examined by DPPH and ABTS assay. The results indicated that YT quenches the intrinsic fluorescence of α-glucosidase following a mixed quenching mechanism accompanied by a hydrophobic (ΔS° > 0 and ΔH° > 0), endothermic, spontaneous and entropy-driven process that was mainly Tryptophan gated. The enzyme's structural conformation was compromised, as revealed by synchronous and UV-absorption spectroscopy. The extract showed more potent inhibition against α-glucosidase with an IC50 value of 153 µg/mL and relatively DPPH and ABTS scavenging activity. This study provides preliminary data for the plant's potential use in the management of hyperglycemia and α-glucosidase implicated pathological conditions.