Comparison of α-glucosidase inhibition by Cudrania tricuspidata according to harvesting time

Abstract

Abstract. Cudrania tricuspidata (CT) is a type of add-value beneficial plant. The aim of the present study was to determine the components of CT that inhibit α-glucosidase activity. Roots, leaves and stems of the plants were obtained and several subgroups were created according to harvesting time. Root extracts exhibited a 77% velocity inhibition at a concentration of 300 µg/ml and an inhibitory constant of 41.6 µg/ml. The inhibitory percentage of the positive control at 1 mM was ~67% of the enzymatic velocity with acarbose. According to the Michaelis-Menten equation, the type of inhibitory mechanism underlying the effects of the stem and root samples according to climate was competitive or non-competitive inhibition, suggesting that the extracts contain additional antidiabetic compounds produced during the growth period. Collectively, the results from our study suggested that stem and root extracts of CT serve as an antidiabetic biomaterial and contain a variety of antidiabetic compounds.

Rational in silico design of novel α-glucosidase inhibitory peptides and in vitro evaluation of promising candidates

“…For SVPA, both enzymes were inhibited uncompetitively in the in vitro studies and non-competitively in the molecular docking analyses, while SEPA revealed a non-competitive inhibition in vitro and a competitive inhibition in the molecular docking against α-glucosidase. Also, acarbose, a known competitive inhibitor of αglucosidase was confirmed to exhibit competitive inhibition in the present study with molecular docking analysis but a number of in vitro experiments have also shown that acarbose is a mixed inhibitor [25,26]. These observations demonstrate the need to further validate some of the docking data with in vitro experiments.…”

Identification and functional characterisation of bioactive peptides in rice bran albumin hydrolysates

“…This suggests that peptides in AAIE1 can bind to both enzyme (E) and enzyme–substrate complex (ES), but with different affinities. Interestingly, the mode of action of AAIE1 was the same as that of Acarbose, which is one of the standard prescription drugs for the management diabetes (Son & Lee, ).…”

Rice bran protein hydrolysates exhibit strong in vitro α‐amylase, β‐glucosidase and ACE‐inhibition activities

“…These results suggest that GAIE1 fraction can bind to both the enzyme and the enzyme–substrate complex but with different affinities. The mode of action of GAIE1 was essentially the same as that of acarbose, which also exhibits a mixed non‐competitive mode of action against α ‐glucosidase …”