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Journal of Innovation in Science, Engineering and Technology

Document Type

Original Study

Abstract

Incorporating vegetables with α -amylase inhibitory properties into the diet is a natural and nutritious way to help regulate blood sugar levels, reduce the risk of complications associated with diabetes mellitus, and promote overall health and well-being. However, during the cooking process, the chemical structure of active compounds, which are responsible for α -amylase inhibition, can change. Hence, this was aimed to evaluate the α -amylase inhibition potential of boiled and non-boiled aqueous extracts (BAE and NBAE respectively) of selected vegetables belonging to the Brassica oleracea L species, which are commonly consumed as in fresh salads as well as in curry or fried form i.e. Brassica oleracea L. var. italica (Broccoli; BOI), Brassica oleracea L. var. capitate (White Cabbage; BOC), Brassica oleracea L. var. gongylodes (Kohlrabi; BOG), Brassica oleracea L. var. botrytis (Cauliflower; BOB), by using a spectrophotometric method. The α -amylase inhibition activity of test samples was expressed as an IC50, which is defined as the mean concentration of the sample required to inhibit 50% activity of the enzyme. The BAE of BOI, BOC, BOG and BOB showed inhibition activity with an IC50 value of 392.07 mg/mL, 203.68 mg/mL, 346.38 mg/mL and 41.67 mg/mL, respectively. On the other hand, NBAE of BOI, BOC, BOG and BOB showed 22.17 mg/mL, 104.48 mg/mL, 449.21 mg/mL and 20.42 mg/mL, respectively as their IC50 values. The acarbose, which was the positive standard, showed an IC50 value of 30.08 mg/mL. In conclusion, the present findings demonstrated the dose-dependent in-vitro α -amylase inhibition properties of selected Brassica sp. vegetables in their boiled and non-boiled aqueous extracts. Except for BOG, all other samples showed a significant reduction (p < 0.05) in inhibitory activity on α -amylase when they were boiled. Hence, it is recommended to eat more fresh salad instead of the cooked form to get maximum α -amylase inhibition properties.

First Pages

13

Last Page

25

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