## 2 Results and Discussions
### Bioactive Properties
In general, \(\alpha\)-amylase and \(\alpha\)-glucosidase enzymes are associated with weight gain, calorie intake, and glycemic index values as they are responsible for the digestion of carbohydrates ([PERSON], 2015). ACE is an important enzyme that catalyzes one step of a series of biochemical reactions that can lead to high blood pressure, and ACE inhibitors such as catoppril are used in the treatment of high blood pressure illness ([PERSON] et al., 2015). AChE inhibitors are also used in the treatment of neurodegenerative diseases such as Alzheimer's disease ([PERSON], 2015). However, the in vitro analyses performed here only reflect the enzyme inhibitory potential of HOC and FHOC. Under in vivo conditions, these inhibition effects may be different from the results determined here. In the present study, in accordance with the literature, \(\alpha\)-amylase inhibition was not observed in FHOC (10 mg/mL, pH 7.0), but the FHOC itself had enzyme activity of \(\alpha\)-amylase (17.52 \(\pm\) 0.55 U/mL). The \(\alpha\)-glucosidase enzyme inhibition value of FHOC increased from 10.49 \(\pm\) 0.12 to 182.11 \(\pm\) 2.61 mg acardose/g by fermentation. A very high inhibition increase was observed here (\(p\leq\) 0.05). Although _Aspergillus oryzae_ produces various glucosidase enzymes to hydrolyze complex or polymeric carbohydrates, a study showed that out of 13 different _Aspergillus oryzae_ strains, one extracellular and ten intracellular strains had \(\alpha\)-glucosidase inhibitory activity ([PERSON], 2015). When one of the strains was examined in detail, it was determined that the inhibitory activity increased as the fermentation time increased. As a result of the analysis, it was reported that Cys-Leu and Pro-Phe-Pro peptides showed very high inhibitory effect. In fermented lentil samples produced by SSF using _Aspergillus oryzae_ and _Aspergillus niger_, the \(\alpha\)-glucosidase inhibition activity decreased over time in the samples in which _Aspergillus oryzae_ was used during fermentation, while the inhibition activity increased over time in the medium in which _Aspergillus niger_ was used. In that study, the inhibitory effect was attributed to the presence of bioactive peptides in the medium ([PERSON], 2015). In another study, the increased \(\alpha\)-glucosidase inhibition activity in mulberry fermentation using _Aspergillus oryzae_, _Aspergillus niger_, and _Monascus anka_ was associated with aglycone phenolic compounds (quercetin and kaempfer) ([PERSON], 2015). A similar approach was reported for the increased inhibitory effect of black tea fermentation ([PERSON], 2015). A 43% decrease in ACE inhibition activity of FHOC was observed after fermentation. ACE inhibition activity is generally associated with the binding of biomolecules such as polyphenols, flavonoids and bioactive peptides to the active site of the enzyme, thereby reducing enzymatic activity [115]. Most studies in this field have been carried out with bioactive peptides produced from milk proteins, and the results have shown that short-chain peptides are most likely to exhibit high antihypertensive activity if they have proline, lysine, or arginine amino acids at their C-terminal ends. For long-chain peptides, it has been reported that the last four amino acids at the C-terminus are decisive in antihypertensive effect [116]. They reported significant increases in the amount and activity of antihypertensive peptides in soybeans fermented using _Aspergillus oryzae_[117]. Similar to our study, in 12 buckwheat floors fermented using 13 different lactic acid bacteria, decreases in ACE inhibition activities were observed in varying ratios compared to the control sample [118]. [PERSON] et al. (2019) reported that during tempel production from legumes, ACE inhibition activity in the medium increased until the 3 rd day of fermentation, then decreased sharply [119].