Evaluation of Carbonic Anhydrase, Acetylcholinesterase, Butyrylcholinesterase, and α-Glycosidase Inhibition Effects and Antioxidant Activity of Baicalin Hydrate

Abstract

Baicalin is the foremost prevalent flavonoid found in Scutellaria baicalensis. It also frequently occurs in many multi-herbal preparations utilized in Eastern countries. The current research has assessed and compared the antioxidant, antidiabetic, anticholinergic, and antiglaucoma properties of baicalin hydrate. Baicalin hydrate was tested for its antioxidant capacity using a variety of techniques, including N,N-dimethyl-p-phenylenediamine dihydrochloride radical (DMPD•+) scavenging activity, 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulphonate) radical (ABTS•+) scavenging activity, 1,1-diphenyl-2-picrylhydrazyl radical (DPPH•) scavenging activity, potassium ferric cyanide reduction ability, and cupric ions (Cu2+) reducing activities. Also, for comparative purposes, reference antioxidants, such as butylated hydroxyanisole (BHA), Trolox, α-Tocopherol, and butylated hydroxytoluene (BHT) were employed. Baicalin hydrate had an IC50 value of 13.40 μg/mL (r2: 0.9940) for DPPH radical scavenging, whereas BHA, BHT, Trolox, and α-Tocopherol had IC50 values of 10.10, 25.95, 7.059, and 11.31 μg/mL for DPPH• scavenging, respectively. These findings showed that baicalin hydrate had comparably close and similar DPPH• scavenging capability to BHA, α-tocopherol, and Trolox, but it performed better than BHT. Additionally, apart from these studies, baicalin hydrate was tested for its ability to inhibit a number of metabolic enzymes, including acetylcholinesterase (AChE), butyrylcholinesterase (BChE), carbonic anhydrase II (CA II), and α-glycosidase, which have been linked to several serious illnesses, such as Alzheimer’s disease (AD), glaucoma, and diabetes, where the Ki values of baicalin hydrate toward the aforementioned enzymes were 10.01 ± 2.86, 3.50 ± 0.68, 19.25 ± 1.79, and 26.98 ± 9.91 nM, respectively.

Detoxifying Cyanides Using Cyanase Enzyme Complexes Composed of Carbonic Anhydrase via Irreversible Covalent Bonds

“…Thus, carbonic anhydrase, which converts carbon dioxide and water into HCO 3 – , − was utilized with cyanase in this study (Figure ). Carbonic anhydrase active moieties typically contain Zn 2+ and are classified as metalloenzymes . There are eight types in total: α, β, γ, δ, ζ, η, θ-, and ι-CAs. ,, Among these, the α form found in animals has been the most extensively studied.…”

“…Carbonic anhydrase active moieties typically contain Zn 2+ and are classified as metalloenzymes. 21 There are eight types in total: α, β, γ, δ, ζ, η, θ-, and ι-CAs. 20,22,23 Among these, the α form found in animals has been the most extensively studied.…”