Prenatal and Postnatal Nutrition Influence Pancreatic and Intestinal
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The Distribution of Carbohydrase Activities in the Small Intestine in Early Weaned Calves
The Distribution of Carbohydrase Activities in the Small Intestine in Early Weaned Calves Toshikazu MIYASHIGEand Shigefusa YAHATA Chugoku National Agricultural Experiment Station, Oda-shi 694-01 (Received December 8, 1980) Abstract 1. The carbohydrase activities of the small intestine of early weaned calves were compared with those of nursing ones at 26 weeks of age. 2. In the early weaned calves, the pH value of content of the caecum was observed to be lower than that of the nursing ones, suggesting that more soluble carbohydrates would have escaped from ruminal fermentation and reached the caecum. 3. The values of maltase and iso maltase activities of the early weaned calves were not different from those of the nursing ones. However, maltase activity of the early weaned calves distributed more constantly with relatively high level all over the small intestine. Lactase activity of the early weaned calves was almost the same as that of the nursing ones. Dextranase and amylase activities were also found in the small intestine of the early weaned calves. Jpn. J. Zootech. Sci., 52 (7): 532-536, 1981 In the previous study1) with nursing calves, it was shown that intestinal maltase activity was very low and did not increase with age. But the pattern of the distri- bution of maltase activity in the small intestine apparently changed with age and higher activity of maltase was found in the lower part of the small intestine at 26 weeks of age. Although the meaning of this change is not known, it is supposed that the change of the pattern would be correlated with the increase of solid food intake. -
SI Gene Sucrase-Isomaltase
SI gene sucrase-isomaltase Normal Function The SI gene provides instructions for producing the enzyme sucrase-isomaltase. This enzyme is found in the intestinal tract, where it is involved in breaking down the sugars sucrose (a sugar found in fruits, and also known as table sugar) and maltose (the sugar found in grains). Sucrose and maltose are called disaccharides because they are each made up of two simple sugar molecules. Disaccharides must be broken down into simple sugar molecules to be digested properly. The sucrase-isomaltase enzyme is found on the surface of the intestinal epithelial cells, which are cells that line the walls of the intestine. These cells have fingerlike projections called microvilli that absorb nutrients from food as it passes through the intestine. Based on their appearance, groups of these microvilli are known collectively as the brush border. The role of the sucrase-isomaltase enzyme is to break down sucrose and maltose into simple sugars so that they can be absorbed by microvilli into intestinal epithelial cells. Health Conditions Related to Genetic Changes Congenital sucrase-isomaltase deficiency At least 10 mutations in the SI gene have been found to cause congenital sucrase- isomaltase deficiency. These mutations disrupt the folding and processing of the sucrose-isomaltase enzyme, transportation of the enzyme within the intestinal epithelial cells, the orientation of the enzyme to the cell surface, or its normal functioning. An impairment in any of these cell processes results in a sucrase-isomaltase enzyme that cannot effectively break down sucrose, maltose, or other compounds made from these sugar molecules (carbohydrates). -
Effect of a Multi-Carbohydrase and Phytase Complex on the Ileal And
animals Article Effect of a Multi-Carbohydrase and Phytase Complex on the Ileal and Total Tract Digestibility of Nutrients in Cannulated Growing Pigs 1, 2, 1, 1 1 3 Jia-Cheng Yang y, Li Wang y, Ya-Kuan Huang y, Lei Zhang , Rui Ma , Si Gao , Chang-Min Hu 4, Jlali Maamer 5, Cozannet Pierre 5, Aurélie Preynat 5, Xin Gen Lei 6 and Lv-Hui Sun 1,* 1 Department of Animal Nutrition and Feed Science, College of Animal Science and Technology, Huazhong Agricultural University, Wuhan 430070, China; [email protected] (J.-C.Y.); [email protected] (Y.-K.H.); [email protected] (L.Z.); [email protected] (R.M.) 2 Institute of Animal Science, Guangdong Academy of Agricultural Sciences, Guangzhou 510640, China; [email protected] 3 Demonstration Center of Hubei Province for Experimental Animal Science Education, Huazhong Agricultural University, Wuhan 430070, China; [email protected] 4 College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, China; [email protected] 5 Adisseo France S.A.S., Center of Expertise in Research and Nutrition, 03600 Commentry, France; [email protected] (J.M.); [email protected] (C.P.); [email protected] (A.P.) 6 Department of Animal Science, Cornell University, Ithaca, NY 14853, USA; [email protected] * Correspondence: [email protected]; Tel.: +86-130-0712-1983 These authors contributed equally to this work. y Received: 6 July 2020; Accepted: 14 August 2020; Published: 17 August 2020 Simple Summary: It is well accepted that monogastric livestock lack phytase in their gastrointestinal tracts. -
Exogenous Enzymes As Zootechnical Additives in Animal Feed: a Review
catalysts Review Exogenous Enzymes as Zootechnical Additives in Animal Feed: A Review Brianda Susana Velázquez-De Lucio 1, Edna María Hernández-Domínguez 1, Matilde Villa-García 1, Gerardo Díaz-Godínez 2, Virginia Mandujano-Gonzalez 3, Bethsua Mendoza-Mendoza 4 and Jorge Álvarez-Cervantes 1,* 1 Cuerpo Académico Manejo de Sistemas Agrobiotecnológicos Sustentables, Posgrado Biotecnología, Universidad Politécnica de Pachuca, Zempoala 43830, Hidalgo, Mexico; [email protected] (B.S.V.-D.L.); [email protected] (E.M.H.-D.); [email protected] (M.V.-G.) 2 Centro de Investigación en Ciencias Biológicas, Laboratorio de Biotecnología, Universidad Autónoma de Tlaxcala, Tlaxcala 90000, Tlaxcala, Mexico; [email protected] 3 Ingeniería en Biotecnología, Laboratorio Biotecnología, Universidad Tecnológica de Corregidora, Santiago de Querétaro 76900, Querétaro, Mexico; [email protected] 4 Instituto Tecnológico Superior del Oriente del Estado de Hidalgo, Apan 43900, Hidalgo, Mexico; [email protected] * Correspondence: [email protected]; Tel.: +52-771-5477510 Abstract: Enzymes are widely used in the food industry. Their use as a supplement to the raw Citation: Velázquez-De Lucio, B.S.; material for animal feed is a current research topic. Although there are several studies on the Hernández-Domínguez, E.M.; application of enzyme additives in the animal feed industry, it is necessary to search for new Villa-García, M.; Díaz-Godínez, G.; enzymes, as well as to utilize bioinformatics tools for the design of specific enzymes that work in Mandujano-Gonzalez, V.; certain environmental conditions and substrates. This will allow the improvement of the productive Mendoza-Mendoza, B.; Álvarez-Cervantes, J. -
Congenital Sucrase-Isomaltase Deficiency
Congenital sucrase-isomaltase deficiency Description Congenital sucrase-isomaltase deficiency is a disorder that affects a person's ability to digest certain sugars. People with this condition cannot break down the sugars sucrose and maltose. Sucrose (a sugar found in fruits, and also known as table sugar) and maltose (the sugar found in grains) are called disaccharides because they are made of two simple sugars. Disaccharides are broken down into simple sugars during digestion. Sucrose is broken down into glucose and another simple sugar called fructose, and maltose is broken down into two glucose molecules. People with congenital sucrase- isomaltase deficiency cannot break down the sugars sucrose and maltose, and other compounds made from these sugar molecules (carbohydrates). Congenital sucrase-isomaltase deficiency usually becomes apparent after an infant is weaned and starts to consume fruits, juices, and grains. After ingestion of sucrose or maltose, an affected child will typically experience stomach cramps, bloating, excess gas production, and diarrhea. These digestive problems can lead to failure to gain weight and grow at the expected rate (failure to thrive) and malnutrition. Most affected children are better able to tolerate sucrose and maltose as they get older. Frequency The prevalence of congenital sucrase-isomaltase deficiency is estimated to be 1 in 5, 000 people of European descent. This condition is much more prevalent in the native populations of Greenland, Alaska, and Canada, where as many as 1 in 20 people may be affected. Causes Mutations in the SI gene cause congenital sucrase-isomaltase deficiency. The SI gene provides instructions for producing the enzyme sucrase-isomaltase. -
Collection of Information on Enzymes a Great Deal of Additional Information on the European Union Is Available on the Internet
European Commission Collection of information on enzymes A great deal of additional information on the European Union is available on the Internet. It can be accessed through the Europa server (http://europa.eu.int). Luxembourg: Office for Official Publications of the European Communities, 2002 ISBN 92-894-4218-2 © European Communities, 2002 Reproduction is authorised provided the source is acknowledged. Final Report „Collection of Information on Enzymes“ Contract No B4-3040/2000/278245/MAR/E2 in co-operation between the Federal Environment Agency Austria Spittelauer Lände 5, A-1090 Vienna, http://www.ubavie.gv.at and the Inter-University Research Center for Technology, Work and Culture (IFF/IFZ) Schlögelgasse 2, A-8010 Graz, http://www.ifz.tu-graz.ac.at PROJECT TEAM (VIENNA / GRAZ) Werner Aberer c Maria Hahn a Manfred Klade b Uli Seebacher b Armin Spök (Co-ordinator Graz) b Karoline Wallner a Helmut Witzani (Co-ordinator Vienna) a a Austrian Federal Environmental Agency (UBA), Vienna b Inter-University Research Center for Technology, Work, and Culture - IFF/IFZ, Graz c University of Graz, Department of Dermatology, Division of Environmental Dermatology, Graz Executive Summary 5 EXECUTIVE SUMMARY Technical Aspects of Enzymes (Chapter 3) Application of enzymes (Section 3.2) Enzymes are applied in various areas of application, the most important ones are technical use, manufacturing of food and feedstuff, cosmetics, medicinal products and as tools for re- search and development. Enzymatic processes - usually carried out under mild conditions - are often replacing steps in traditional chemical processes which were carried out under harsh industrial environments (temperature, pressures, pH, chemicals). Technical enzymes are applied in detergents, for pulp and paper applications, in textile manufacturing, leather industry, for fuel production and for the production of pharmaceuticals and chiral substances in the chemical industry. -
Digestion of Carbohydrates
Digestion of carbohydrates Alongside fat and protein, carbohydrates are one of the three macronutrients in our diet with their main function being to provide energy to the body. They occur in many different forms, like sugars and dietary fibre, and in many different foods, such as whole grains, fruit and vegetables. Digesting or metabolizing carbohydrates breaks foods down into sugars, which are also called saccharides. These molecules begin digesting in the mouth and continue through the body to be used for anything from normal cell functioning to cell growth and repair. It is also directly used as energy source in muscle, brain and other cells. Dietary carbohydrate principally consists of …. Polysaccharides: - Starch, glycogen and cellulose Disaccharides: - Sucrose and maltose Monosaccharide:-Glucose and fructose Out of these three types of carbohydrates, monosaccharide does not need digestion. Digestion of carbohydrates During digestion, carbohydrates that consist of more than one sugar get broken down into their monosaccharides by digestive enzymes, and then get directly absorbed causing a glycaemic response. Some of the carbohydrates cannot be broken down and they get either fermented by our gut bacteria or they transit through the gut without being changed. Digestive enzymes and their source Mouth: - Salivary amylase (α-amylase, Ptyalin) Stomach: - No enzymes Pancreas: - Pancreatic α-amylase Intestine: - Dextrinase, Maltase, Isomaltase, Sucrase, Lactase Digestion in mouth Digestion of carbohydrates starts at the mouth. In mouth, -
Biochemical Characterization of Digestive Carbohydrases in the Rose Sawfly, Arge Rosae Linnaeus (Hymenoptera: Argidae)
J. Crop Prot. 2013, 2 (3): 305-318 ______________________________________________________ Biochemical characterization of digestive carbohydrases in the rose sawfly, Arge rosae Linnaeus (Hymenoptera: Argidae) Moloud Gholamzadeh Chitgar1, Seyed Mohammad Ahsaei2, Mohammad Ghadamyari1*, Mahbobe Sharifi1, Vahid Hosseini Naveh2 and Hadi Sheikhnejad1 1. Department of Plant Protection, Faculty of Agricultural Science, University of Guilan, Rasht, Iran. 2. Department of Plant protection, Faculty of Agricultural Sciences & Engineering, College of Agriculture and Natural Resources, University of Tehran, Karaj, Iran. Abstract: The rose sawfly, Arge rosae Linnaeus, is one of the most destructive pests of rose bushes in the north of Iran. Nowadays, many attempts have been made to reduce pesticide application by looking for new methods of pest control. A non chemical method for controlling insect pests including A. rosae can be achieved by using genetically engineered plants expressing carbohydrase inhibitors. Therefore, in present study we characterized biochemical properties of digestive carbohydrases in the gut of A. rosae for achieving a new method for control of this pest. The specific activity of α-amylase in the digestive system of last larval instars of A. rosae was obtained as 9.46 ± 0.06 μmol min-1 mg-1 protein. Also, the optimal pH and temperature for α-amylase were found to be at pH 8 and 50 °C. As calculated from Lineweaver-Burk plots, the Km and Vmax values for α-amylase were 0.82 mg/ml and 7.32 µmol min-1 mg-1 protein, respectively, when starch was used as substrate. The effects of ions on amylolytic activity showed that Mg2+ and Na+ significantly increased amylase activity, whereas SDS and EDTA decreased the enzyme activity. -
The Mechanism of Carbohydrase Action 5
246 Biochem. J. (1960) 76, 246 The Mechanism of Carbohydrase Action 5. ACTION OF HUMAN SALIVARY a-AMYLASE ON AMYLOPECTIN AND GLYCOGEN* By P. J. P. ROBERTSt AND W. J. W-HELANt Chemistry Department, University College of North Wales, Bangor (Received 11 January 1960) When human salivary oc-amylase acts on whole if any, esterified phosphorus (Schoch, 1953). It was pre- starch (amylose+amylopectin) there is produced pared from hand-sorted single-cross Tapicorn seed, (Bear a mixture of fermentable and unfermentable Hybrid Co., Decatur, Illinois, U.S.A.) as by Schoch (1957). sugars (Myrback, 1948). The fermentable sugars Buffers. These were 0-2 m-sodium acetate-acetic acid consist of maltose, maltotriose and/or glucose (see (pH 7.0) and 0-2M-sodiunm citrate-citric acid (pH 7-0). below). The non-fermentable sugars (a-limit Methods dextrins) are a mixture of higher oigosaccharides. Digests. Waxy-maize starch was moistened with ethanol Since the amylose component of starch, which and dissolved in 0-6N-sodium hydroxide by heating in a consists essentially only of 1:4-linked a-glucose boiling-water bath for 5 min. After cooling, the alkali was units, can be converted by the amylase completely neutralized to phenolphthalein either with sulphuric acid into maltose and maltotriose (Whelan & Roberts, [digests (1) and (2), see below] or hydrochloric acid [digest 1953) the a-limit dextrins must arise from the (3)]. Glycogen and the enzymes were dissolved in water. amylopectin component and may be assumed to After the substrate had dissolved, the buffer was added and contain the a-1:6-bonds which constitute the points then the enzyme. -
Sucraid Review
TAB B United States CONSUMER PRODUCT SAFETY COMMISSION Washington, D.C. 20207 APR I 1998 MEMORAh?)UM TO: Mary Ann Danello, Ph.D., Associate Executive Director, Directorate for Epidemiology and Health Sciences THROUGH: Marilyn L. Wind, Ph.D., Director, Division of Health Sciences,w&; Directorate for Epidemiology and Health Sciences FROM: Jacqueline N. Ferrante, Ph.D., Pharmacologist, Division of Health Sciences, JF Directorate for Epidemiology and Health Sciences SUBJECT: Sucraid Review 1 Introduction Orphan Medical petitioned the Commission to exempt SucraidrM, an oral solution of the enzyme sacrosidase, from special packaging requirements for oral prescription drugs under the Poison Prevention Packaging Act (PPPA). This memorandum reviews scientific information related to Sucraidr”. Product Description and Use SucraidTM is the brand name for sacrosidase, a yeast-derived form of the sucrase enzyme. This enzyme is obtained from baker’s yeast which is also known as Saccharomyces cerevisiae. SucraidTM contains 1.5 milligrams (8,500 International Units) per milliliter (mg/ml) of the enzyme in a 5050 solution of glycerol and water at an unbuffered slightly acidic pH of 4.6. SucraidTM is the only available treatment for congenital sucrase-isomaltase deficiency (CSID). It is replacement therapy for sucrase, not isomaltase. The petitioner argues that the confectionery and baking industry has used this enzyme extensively and that under 21 CFR 170.30 it is a “Generally Recognized as Safe” (GRAS) food material because of its long history of safe use in humans. It is used as a flavoring agent and adjuvant at a level not to exceed five percent in food. The recommended dose of SucraidTM for patients with CSID is one ml per meal or snack for patients weighing up to 15 kilograms (kg) (33 pounds) and 2 ml for patients over 15 kg. -
CSID) Symptoms, Diagnosis, and Treatment
CONGENITAL SUCRASE-ISOMALTASE DEFICIENCY (CSID) Symptoms, Diagnosis, and Treatment FOR ADULT GASTROENTEROLOGISTS PMS 294 2020 QOL Medical, LLC 1 Financial Disclosures o [Disclose financial relationships with manufacturers and medical organizations here (e.g., QOL Medical, LLC); if none, list “None.”] PMS 294 2020 QOL Medical, LLC 2 WHAT IS CSID? PMS 294 2020 QOL Medical, LLC 3 CSID: Congenital Sucrase-Isomaltase Deficiency Sucrase-Isomaltase o An enzyme that digests the majority of dietary carbohydrates o Table sugar (sucrose) and many starches (e.g., potatoes, bread) o Expressed in the microvilli of the brush border membrane o Releases glucose and fructose from sucrose (sugar) so they can be absorbed into the bloodstream PMS 294 2020 QOL Medical, LLC 4 Congenital Sucrase-Isomaltase Deficiency The first report of an autosomal recessive Congenital Sucrase-Isomaltase Deficiency (CSID) was published in 1960. Diarrhoea Caused by Deficiency of Sugar-Splitting Enzymes Weijers HA, Van De Kamer JH, Mossel DAA, Dicke WK. Diarrhoea Caused by Deficiency of Sugar-Splitting Enzymes. Lancet. 1960;276(7145):296-7. PMS 294 2020 QOL Medical, LLC 5 Sucrase-Isomaltase Substrates Sucrose Isomaltose Glucose + Fructose Glucose + Glucose (a-1,2 glycosidic bond) (a-1,6 glycosidic bond) PMS 294 2020 QOL Medical, LLC 6 How Sucrase Works to Hydrolyze Sucrose 1. Enzyme Substrate binds to disaccharide (Sucrose) substrate Enzyme H20 (Sucrase) 4. Active site available for another substrate 3. Products are released and absorbed 2. Substrate is converted to monosaccharides Glucose Fructose PMS 294 2020 QOL Medical, LLC 7 CSID Carb Maldigestion Pathophysiology NORMAL CSID PMS 294 2020 QOL Medical, LLC 8 SI Gene o Encodes a heterodimer with 2 active sites – sucrase and isomaltase • Located on chromosome 31 • Very large – approximately 100 kilobases1 • 48 exons encoding 1827 amino acids1 o 2146 rare variants with 880 SI rare pathogenic variants (SI-RPVs)2 • Sucrase-Isomaltase protein transported and anchored to apical membrane of enterocytes to digest disaccharides in intestinal lumen3 1. -
Functional Variants in the Sucrase–Isomaltase Gene Associate With
Gut Online First, published on November 21, 2016 as 10.1136/gutjnl-2016-312456 Neurogastroenterology ORIGINAL ARTICLE Gut: first published as 10.1136/gutjnl-2016-312456 on 21 November 2016. Downloaded from Functional variants in the sucrase–isomaltase gene associate with increased risk of irritable bowel syndrome Maria Henström,1 Lena Diekmann,2 Ferdinando Bonfiglio,1 Fatemeh Hadizadeh,1 Eva-Maria Kuech,2 Maren von Köckritz-Blickwede,2 Louise B Thingholm,3 Tenghao Zheng,1 Ghazaleh Assadi,1 Claudia Dierks,4 Martin Heine,2 Ute Philipp,4 Ottmar Distl,4 Mary E Money,5,6 Meriem Belheouane,7,8 Femke-Anouska Heinsen,3 Joseph Rafter,1 Gerardo Nardone,9 Rosario Cuomo,10 Paolo Usai-Satta,11 Francesca Galeazzi,12 Matteo Neri,13 Susanna Walter,14 Magnus Simrén,15,16 Pontus Karling,17 Bodil Ohlsson,18,19 Peter T Schmidt,20 Greger Lindberg,20 Aldona Dlugosz,20 Lars Agreus,21 Anna Andreasson,21,22 Emeran Mayer,23 John F Baines,7,8 Lars Engstrand,24 Piero Portincasa,25 Massimo Bellini,26 Vincenzo Stanghellini,27 Giovanni Barbara,27 Lin Chang,23 Michael Camilleri,28 Andre Franke,3 Hassan Y Naim,2 Mauro D’Amato1,29,30 ▸ Additional material is ABSTRACT published online only. To view Objective IBS is a common gut disorder of uncertain Significance of this study please visit the journal online (http://dx.doi.org/10.1136/ pathogenesis. Among other factors, genetics and certain gutjnl-2016-312456). foods are proposed to contribute. Congenital sucrase– isomaltase deficiency (CSID) is a rare genetic form of What is already known on this subject? disaccharide malabsorption characterised by diarrhoea, ▸ fi fi IBS shows genetic predisposition, but speci c For numbered af liations see abdominal pain and bloating, which are features end of article.