通过抑制α-葡萄糖苷酶和α-淀粉酶评估帕利叶乙醇馏分(Kleinhovia hospita L)的抗糖尿病活性

Sarniati Rante Rura, Y. Djabir, Abdul Rahim, Sri Ningsih, N. Firdausi
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摘要

Kleinhovia hospita长期以来一直被用于治疗疾病,包括糖尿病。本研究旨在评估 K. hospita 提取物和馏分的降血糖作用是否与其抑制α-淀粉酶和α-糖苷酶的活性有关。K. hospita叶片用96%乙醇提取,然后以正己烷、乙酸乙酯和水为溶剂进行液-液分配。测试了乙醇提取物及其馏分对α-淀粉酶和α-糖苷酶酶活性的抑制能力,并与阿卡波糖进行了比较。体外研究表明,乙醇提取物、己烷、乙酸乙酯和水馏分对α-淀粉酶活性的 IC50 分别为 1496.8 µg/mL、1266.7 µg/mL、12577.5 µg/mL和 5217.0 µg/mL。而对于α-糖苷酶活性,IC50 值分别为 1341.2 微克/毫升、25470.0 微克/毫升、64450.0 微克/毫升和 1291.4 微克/毫升。这些数值明显高于阿卡波糖(分别为 7.4 微克/毫升和 5.5 微克/毫升)。研究结果表明,K. hospita 叶提取物和馏分的 IC50 值较高,这表明 K. hospita 的降血糖作用与抑制α-淀粉酶和α-糖苷酶无关。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Evaluation of the Anti-Diabetic Activity of Paliasa Leaf Ethanol Fraction (Kleinhovia hospita L) Through Inhibition of the Enzymes $\alpha$-Glucosidase and $\alpha$-Amylase
Kleinhovia hospita has long been used to treat diseases, including diabetes mellitus. This study aimed to evaluate if the hypoglycemic effects of K. hospita extract and fractions were related to its inhibition on the activity of $\alpha$-amylase and $\alpha$-glycosidase enzymes. K. hospita leaves were extracted with 96% ethanol and then subjected to liquid-liquid partition using n-hexane, ethyl acetate, and water as solvents. The inhibitory capacity of ethanolic extract and its fractions were tested against $\alpha$-amylase and $\alpha$-glycosidase enzyme activity and compared to acarbose. The in vitro study revealed that the IC50 of ethanolic extract, hexane, ethyl acetate, and water fractions were 1496,8 µg/mL, 1266,7 µg/mL, 12577,5 µg/mL, and 5217,0 µg/mL, respectively, against alfa-amylase activity. Whereas, for $\alpha$-glycosidase activity, the IC50 values were 1341,2 µg/mL, 25470,0 µg/mL, 64450,0 µg/mL, and 1291,4 µg/mL, respectively. These values were markedly greater than those of the acarbose (7,4 and 5,5 µg/mL, respectively). From the research results, it was concluded that K. hospita leaf extract had a high IC50 value from K. hospita extracts and fractions, which indicated that the hypoglycemic effect of K. hospita was not related to the inhibition of the $\alpha$-amylase and $\alpha$-glycosidase enzymes.
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