α-L-fucosidase (AFU) is an acid hydrolase that exists in organisms and widely exists in tissues, cells, blood and body fluids. AFU is involved in the metabolism of glycoproteins, glycolipids and oligosaccharides, and plays a key role in cell differentiation, apoptosis, inflammation and host-pathogen interaction. AFU catalyzes the hydrolysis of the colorless substrate nitrophenyl-α-L-fucoside to produce yellow nitrophenol with a significant absorption peak at 405 nm, and its absorbance is positively correlated with the content of nitrophenol. The activity of AFU can be calculated by measuring the change of absorbance value at 405 nm.
β-1, 3-glucanase (β-1,3-GA, EC 3.2.1.39) is mainly found in plants and catalyzes the hydrolysis of β-1, 3-glucosidic bonds, thereby destroying fungal cell walls. In particular, when synergistic with chitinase, it can significantly inhibit the growth of fungi. When plants are infected with diseases or under other stress conditions, they can induce a large amount of β-1, 3-GA to enhance plant resistance to adverse external stimuli. Therefore, the determination of β-1, 3-GA activity is widely used in plant pathology and stress physiology research. β-1,3-GA hydrolyses the β-1, 3-glucosidic linkage of laminarin to produce reducing ends. The activity can be reflected by measuring the amount of reducing sugar using 3, 5-dinitrosalicylic acid.
The reducing sugar reacts with 3,5-dinitrosalicylic acid under heating conditions to produce a brown-red substance. β-amylase was inactivated by the property of amylase not to be heat-resistant, and then the enzyme activity of total amylase and α-amylase is determined. So the activity of β-amylase can be calculated indirectly.
β-galactosidase can catalyze the substrate nitrophenylgalactoside pyranopyranoside to produce nitrophenol, which has a maximum absorption peak at 400 nm. The activity of β-GAL can be calculated by measuring the OD value at 400 nm.
β-glucosidase (β-GC), also known as β-glucoside hydrolase, can efficiently hydrolyze the terminal non-reducing β-D-glucoside bonds in various glycoside compounds, thereby releasing β-D-glucose and corresponding ligands. The enzyme is widely present in nature, including the seeds of various plants, the small intestine and other organs of animals, and microorganisms. β-GC is a very important industrial enzyme with various applications. In the field of medicine, β-GC catalyzes the degradation of glycoside groups to inhibit the expansion of cancer cells. In terms of diet, β-GC catalyzes the production of anti-cancer molecules isoflavones in soybean. In the energy field, β-GC is one of the key enzymes in the conversion of cellulose to glucose. β-GC catalyzed the reaction of substrate to produce chromogenic substances at the wavelength of 400 nm, the maximum absorption of β-GC enzyme activity was reflected by measuring the OD value at 400 nm.
β- hydroxybutyrate dehydrogenase can catalyze the oxidative dehydrogenation of β-HB. Meanwhile, NAD+ is reduced to NADH, Which under the action of hydrogen transmitter, transfer electrons to WST-8 to produce the yellow product. The content of β-HB can be calculated by measuring the change of absorbance value at 450 nm.
β-N-Acetylglucosaminidase (NAG) catalyzed the substrate to produce p-nitrophenol, which has an absorption wavelength at 400 nm. Therefore, the activity of NAG can be calculated by measuring the change of absorbance value at 400 nm.
β-Secretase 1 is an aspartic protease, the full name is β-site amyloid precursor protein cleavage enzyme 1(BACE 1). BACE 1 cleaves amyloid precursor protein (APP) to produce amyloid-β peptide (Aβ) of 40 or 42 amino acids. The deposition of Aβ in plaques and vessel walls in the brains of patients with Alzheimer's disease is widely believed to be the major contributor to the disease. The detection principle of this kit is fluorescence resonance energy transfer (FRET) method. A fluorescence donor group and a quenching group are divided at both ends of the substrate. The fluorescence energy is transferred from the fluorescence donor to the quenching group, resulting in the attenuation of the fluorescence intensity of the fluorescence donor molecule itself. When the substrate is cleaved by BACE 1, the quenching group of the substrate and the fluorescent donor are separated and the fluorescent donor is no longer quenched, the fluorescence of the fluorescent donor can be detected, so that the enzymatic activity of BACE 1 can be calculated. The fluorescence produced by this kit had a maximum excitation wavelength of 325 nm and a maximum absorption wavelength of 393 nm.
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