# Effect of Different Drying Methods on the Quality of _Oudemansiella raphanipes_
## 3 Results and Analysis
### Inhibitory Activity Analysis of PS-V, PS-H and PS-I  
As an essential enzyme in the glucose metabolism pathway in organisms, \(\alpha\)-glucosidase is located on the surface membrane of intestinal cells, where it hydrolyzes glycosidic bonds in carbohydrates and disaccharides (e.g., sucrose, maltose) and releases glucose and other monosaccharides, which are then taken up by the intestinal epithelial cells, leading to elevated blood glucose levels [57]. Thus, the inhibition of \(\alpha\)-glucosidase activity can effectively control postprandial blood glucose levels. As shown in Figure 7A, PS-H, PS-I, and PS-V all have a significant inhibitory effect on the activity of \(\alpha\)-glucosidase, and this effect is dose-dependent. The inhibitory activity of PS-V is consistently higher than the other two. The IC50 values of PS-V, PS-I, and PS-H are 3.881, 2.058, and 0.973 mg\(\cdot\)mL-1, respectively. PS-H and PS-I showed lower inhibition of \(\alpha\)-glucosidase compared to PS-V. This may be due to the hardening of the structure due to internal moisture migration during drying, agglomeration, and possible damage to thermosensitizers and volatile components, as well as disruption of the network structure by temperature, which affects the inhibitory effect on \(\alpha\)-glucosidase. While vacuum freeze-drying treatment inhibits the action of microorganisms and enzymes by drying at low temperatures, while maximizing the retention of the raw material's original network structure and morphology, it has a better inhibition of \(\alpha\)-glucosidase. Meanwhile, [PERSON] et al. and [PERSON] et al. [58; 59] speculate that the polysaccharides have an impact on the changes in inhibition of \(\alpha\)-glucosidase, which may be related to molecular weight distribution and uronic acid content. After degradation, polysaccharides can be absorbed by the small intestine and inhibit intestinal growth. \(\alpha\)-glucosidase actively reduces the risk of postprandial hyperglycemia [60].  
Figure 6: Effect of different drying methods on vitro antioxidant activity of polysaccharides, (**A**) DPPH radical scavenging capacity and (**B**) \(\cdot\)OH radical scavenging capacity. Data are expressed as the mean \(\pm\) standard deviation (\(n=3\)).  
\(\alpha\)-Amylase is, likewise, an important digestive enzyme in the breakdown of carbohydrates by the organism, and it catalyzes the cleavage of the \(\alpha\)-D-(1-4) glycosidic bond of starch and various maltodext into oligosaccharides. As shown in Figure 7B, PS-H, PS-I, and PS-V also exhibit dose-dependent inhibitory activity on \(\alpha\)-amylase. The inhibitory rate of PS-V at all concentrations is higher than the other two. The IC50 values of PS-V, PS-I, and PS-H are 0.938, 0.685, and 0.503 mg\(\cdot\)mL\({}^{-1}\), respectively. In general, polysaccharides may inhibit starch decomposition after entering the body in two ways: First, the polysaccharides may adsorb onto the starch, thereby hindering the decomposition of the starch. Second, some groups in polysaccharides, such as carboxyl groups, may interact with amino acid residues in \(\alpha\)-amylase through hydrogen bonding, thus forming a complex between polysaccharides and \(\alpha\)-amylase, which in turn affects the spatial conformation of \(\alpha\)-amylase. From the figure, it can be seen that PS-V has higher \(\alpha\)-amylase inhibition, which may be due to the fact that the vacuum freeze-drying treatment better maintains the original structure of the polysaccharide to maximize the encapsulation of the enzyme or starch, whereas the structure of the polysaccharide treated by hot air drying and radiation drying degraded during the drying process, which affects the inhibition of \(\alpha\)-amylase activity.