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Therapeutic Potential of Anthocyanin Against Diabetes
Published in Hafiz Ansar Rasul Suleria, Megh R. Goyal, Health Benefits of Secondary Phytocompounds from Plant and Marine Sources, 2021
Tawheed Amin, H. R. Naik, Bazila Naseer, Syed Zameer Hussain
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].
The small intestine
Published in Paul Ong, Rachel Skittrall, Gastrointestinal Nursing, 2017
At birth, the concentrations of the brush border enzymes sucrase and maltase are at mature levels. Both infants and adults require brush border disaccharidases (enzymes) to break down dietary disaccharides to monosaccharides. The high activity of brush border enzymes, glucoamylase, sucrose-isomaltase and lactase, enables them to break down lactose and short-chain glucose polymers. Glucoamylase is an enzyme that breaks the bonds near the ends of complex carbohydrates (starches) releasing maltose and free glucose.
Contact Urticaria, Dermatitis, and Respiratory Allergy Caused by Enzymes
Published in Ana M. Giménez-Arnau, Howard I. Maibach, Contact Urticaria Syndrome, 2014
Stanciu Monica, Denis Sasseville
γ-amylase, also known as glucoamylase and amyloglucosidase, is used in the baking and brewing industry. In 1998, Kanerva and Vanhanen published a case of occupational protein contact dermatitis from this enzyme. [22] They described a 28-year-old chemical enzyme factory worker who developed hand dermatitis 1 hour after exposure to work products. She had a positive prick test, and a negative patch test to glucoamylase.
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.
Discovery of differentially expressed genes in the intestines of Pelteobagrus vachellii within a light/dark cycle
Published in Chronobiology International, 2020
Chuanjie Qin, Jiaxian Sun, Jun Wang, Yongwang Han, He Yang, Qingchao Shi, Yunyun Lv, Peng Hu
The rodent facilitated fructose transporters GLUT, GLUT2, and GLUT5, and the Na-glucose transporter SGLT1, display peak expression at night, and in clock mutant mice (Fatima et al. 2009), however, these nutrient transporters lost their circadian rhythms (Pan and Hussain 2009). Similarly, nile tilapia (Oreochromis niloticus) plasma glucose levels showed a daily rhythm, with the achrophase shifted by 12 h when fed once a day at 11:00 h and at 23:00 h (Guerra-Santos et al. 2016). In the gilthead seabream (Sparus aurata), increased amylase activity was observed a few hours before mealtime with periodic feeding (Montoya et al. 2010). These studies suggested that the transport of glucose in the intestines is regulated rhythmically. In the present study, the maltase-glucoamylase, sucrase-isomaltase, showed regulated expression during the night. Similarly, amylase activity also showed a daily rhythm in the mid-intestines of European sea bass (Dicentrarchus labrax) (del Pozo et al. 2012), and the amylase of tambaqui (Colossoma macropomum) showed a clear daily rhythm when fed at midday or midnight (Silva Reis et al. 2019); however, activity peaked at night. Moreover, similar to rodents, the genes encoding sodium/glucose cotransporters 1 and 4, facilitated glucose transporter member 6-like, and facilitated glucose transporter member 11 showed regulated expression at night. The upregulated expression of these genes suggested that more glucose might be transported from lumen into the blood at night.
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).