Abstract
Chitosan oligosaccharide (COS) is a bioactive compound derived from marine by-products. COS consumption has been demonstrated to lower the risk of diabetes. However, there are limited data on the inhibitory effect of low-molecular-weight COSs with different degrees of polymerization (DP) on α-glucosidase. This study investigates the α-glucosidase inhibitory activity of two low-molecular-weight COSs, i.e., S-TU-COS with DP2−4 and L-TU-COS with DP2−5, both of which have different molecular weight distributions. The inhibition constants of the inhibitors binding to free enzymes (Ki) and an enzyme−substrate complex (Kii) were investigated to elucidate the inhibitory mechanism of COSs with different chain lengths. The kinetic inhibition model of S-TU-COS showed non-completive inhibition results which are close to the uncompetitive inhibition results with Ki and Kii values of 3.34 mM and 2.94 mM, respectively. In contrast, L-TU-COS showed uncompetitive inhibition with a Kii value of 5.84 mM. With this behavior, the IC50 values of S-TU-COS and L-TU-COS decreased from 12.54 to 11.84 mM and 20.42 to 17.75 mM, respectively, with an increasing substrate concentration from 0.075 to 0.3 mM. This suggests that S-TU-COS is a more potent inhibitor, and the different DP of COS may cause significantly different inhibition (p < 0.05) on the α-glucosidase activity. This research may provide new insights into the production of a COS with a suitable profile for antidiabetic activity.