Therapeutic Potential of Anthocyanin Against Diabetes
Hafiz Ansar Rasul Suleria, Megh R. Goyal in Health Benefits of Secondary Phytocompounds from Plant and Marine Sources, 2021
Digestion of carbohydrates inside our body occurs in a successive way with α-amylase acting initially on starch trailed by α-glucosidase to produce dietary glucose. Once the food is ingested, starch is acted upon by α-amylases (both salivary and pancreatic) and four small intestinal mucosal α-glucosidase subunits [57], and at an inner α-1,4 glucosidic linkages via an endo mechanism thereby producing linear and branched maltooligosaccharides [55]. Maltase-glucoamylase and sucrose-isomaltase (the two membrane-bound protein complexes), and mucosal α-glucosidases are exo-type starch hydrolyzing enzymes [65, 68] that produce glucose by hydrolyzingα-1,4 glucosidic linkages opposite to the reducing end of dextrins already degraded by α-amylase [6, 27, 29]. Apart from illustrious maltase activity, the C-terminal subunit (maltase-glucoamylase) is named as isomaltase because of its action on long-chain oligomers [54] whereas the N-terminal subunit (sucrose isomaltase) is named as isomaltase because of its debranching activity [28].
Inhibiting the Absorption of Dietary Carbohydrates and Fats with Natural Products
Christophe Wiart in Medicinal Plants in Asia for Metabolic Syndrome, 2017
Degradation products of starch are hydrolyzed in the jejunum into free absorbable glucose by 4 brush border α-glucosidases arranged into 2 enzymatic complexes termed as sucrase–isomaltase and maltase–glucoamylase.22 Members of the family Menispermaceae often accumulate isoquinoline alkaloids that hamper glucose absorption by inhibiting enterocyte membrane bound α-glucosidases. As an example, Tinospora crispa (L.) Hook. f. & Thomson synthetize palmatine, jatrorrhizine, and magnoflorine that inhibited the enzymatic activity of sucrase with IC50 of 36.2, 23.4, and 9.8 μg/mL, respectively.23 In the same experiment, palmatine, jatrorrhizine, and magnoflorine inhibited the enzymatic activity of maltase with IC50 values equal to 22, 38.4, and 7.6 μg/mL.23 Magnoflorine at a dose of 20 mg/kg mitigated the raise in glycaemia induced by oral administration of 2 g/kg of glucose to rodents.23 Magnoflorine is known to induce hypotension when parenterally administered and to be nontoxic in animals when given orally.24
Weaning: Why, When and What?
Frank Falkner in Infant and Child Nutrition Worldwide:, 2021
Up to the fourth month of life, amylase activity in duodenal fluid is very low or absent (Auricchio et al., 1955; Zoppi et al., 1972), for pancreatic amylase fragments the molecules of starch which results in the production of small polysaccharides, especially maltose and maltotriose. On the other hand, at one month of age there is intestinal glucoamylase hence disaccharides are ready for digestion and the absorption of starches (Lebenthal and Lee, 1980). Normally, starches are hydrolyzed by the action of x-amylase and the later action of maltase and isomaltase in order to be absorbed. In infants, an alternative pathway is the action of glucoamylase that directly hydrolizes starch to glucose. In use of native starches coming from wheat, corn, tapioca, potatoes and rice given to infants during the first months of life, results show that when given as flour cooked for 10 minutes there is 98% absorption (De Vizia et al., 1975). Modified food starches (MFS) have been largely used, added to strained and “junior” foods or soya milk, and act as a good stabilizer and for changing the consistency and texture of the food; its concentration in the food ranges from 5-6.5%. Starches are principally amylopectin and amylose. It has been considered whether the residuals of chemical products employed in the industrial modification of MFS could cause toxic effects; but, The National Academy of Science points out that there is no toxicological basis to exclude MFS in the diet of infants (Filer, 1971). The possibility has also been raised that MFS can chelate minerals, thus interfering with their absorption (Hood and Oshea, 1977). In many products MFS give from 10 to 30% of the total energy, and in vivo and in vitro digestibility studies of corn syrup sugars show that each of the sugars was well hydrolyzed (Lebenthal et al, 1983).
Phytochemical profile, enzyme inhibition activity and molecular docking analysis of Feijoa sellowiana O. Berg
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2021
Fatema R. Saber, Rehab M. Ashour, Ali M. El-Halawany, Mohamad Fawzi Mahomoodally, Gunes Ak, Gokhan Zengin, Engy A. Mahrous
Upon docking in the N-terminal subunit of glucoamylase, the two competitive inhibitors acarbose and miglitol showed multiple H-bond interactions in the active site of the enzyme especially with the acidic residues Asp542, Asp443, Asp327 in addition to Gln603 and His444 (Figure 2(A,B)). Despite being inactive in in vitro assay, avicularin showed similar H-bond pattern through its rings A and C with a good docking score of −6.4146 kcal/mol, (Table 3). Other flavonoids showed different mode of interaction which included some H-bond with active site residues (Arg526, Asp542, Asp203) through ring A and/or aromatic stacking with Trp406 (Figure 2). Similar interactions with acidic amino acids Asp1526, Asp1279, Asp1420 in addition to Arg1510 and His1584 were observed upon docking of acarbose and miglitol in the C-terminal subunit. Docking scores for tested compounds in C-terminal subunit were similar to that of N-terminal subunit as seen in Table 3 and ligand–enzyme interactions followed a similar pattern, Figure S2 (provided in the supplementary file). It is worth mentioning that previous molecular interaction data of flavonoids with α-glucosidases were mainly generated using homology model of Saccharomyces cerevisiae α-glucosidase enzyme, one of the glycoside hydrolase family 31 which is characterised by presence of aspartate residue in their hydrolytic active site34. This is the first report of the molecular interaction of this group of flavonoids in intestinal glucoamylase of the same family showing interaction with the conserved aspartic acid residues in both C and N terminals.
Safety and Efficacy of N-SORB®, a Proprietary KD120 MEC Metabolically Activated Enzyme Formulation: A Randomized, Double-Blind, Placebo-Controlled Study
Published in Journal of the American College of Nutrition, 2019
Qiurong Wang, Rui Guo, Sreejayan Nair, Derek Smith, Bledar Bisha, Anand S. Nair, Rama Nair, Bernard W. Downs, Steve Kushner, Manashi Bagchi
Endogenous digestive enzymes are site- and substrate-specific and mostly activated and work in a pH range of 2 to 5.5 (29). N-SORB is a novel proprietary KD120 MEC metabolically activated enzyme formulation. These enzymes structurally resemble regular digestive enzymes such as amylase, protease, lipase, alpha galactosidase, and glucoamylase. However, N-SORB enzymes function in a pH range between 6.5 and 8.5. This specially engineered enzyme formulation utilizes an exclusive phospholipid (“Prodosome”) encapsulation technology that was shown to promote rapid and sustainable nutrient absorption of nutritional ingredients that effected positive changes in properties of the blood (30). Case studies, and preliminary observations in our laboratories have demonstrated that N-SORB-treated subjects had beneficial effects on their lifestyle. Subjects of different age group (age 20–71 years) have reported significant improvement of gastrointestinal functions, gut health, and increased metabolism without any adverse events. Other benefits include improved digestion, improvement of leaky gut syndrome with less gastrointestinal pain, less fatigue, less bloating, improved bowel movements, and increased energy level (20,21).
Construction, characterization, and bioavailability evaluation of honokiol-loaded porous starch by melting method without any solvent
Published in Drug Delivery, 2021
Apparent solubility was determined by adding an excess of free HK, PM of HK with PS, and the HPS dissolved in buffer solutions with different pH values (1.2(AGJ), 6.8(AIJ), and 5.5), and kept in constant temperature shaker for 48 h at 37 °C. The dissolution mediums contained α-amylase of 1% and glucoamylase of 1%. One milliliter of liquid was were taken out and centrifuged at 10,000 rpm for 10 min, and then filtered through a 0.22 µm membrane filter. The supernatant of the samples was analyzed by the HPLC system after appropriate dilutions in methanol for determining the concentration of HK.
Related Knowledge Centers
- Amylase
- Catalysis
- Chemical Reaction
- Enzyme
- Glycoside Hydrolase Family 15
- Glycoside Hydrolase Family 31
- Maltase-Glucoamylase
- Glycoside Hydrolase Family 97