Sucrase, Maltase and Lactase Activity in the Small Intestine of the Laboratory Wistar Rat, Raised on a Basal Diet

Total Page:16

File Type:pdf, Size:1020Kb

Sucrase, Maltase and Lactase Activity in the Small Intestine of the Laboratory Wistar Rat, Raised on a Basal Diet CERTAIN STUDIES ON THE DIGESTIVE ENZYME SYSTEMS (SUCRASE, MALTASE AND LACTASE) OF THE SMALL INTESTINE OP THE WISTAR RAT by ROBERT JOHN BOSE B.S.A., The University of British Columbia, 1955 A THESIS SUBMITTED IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF MASTER OP SCIENCE IN AGRICULTURE iii the division of Animal Science We accept this thesis as conforming to the required standard Members of the Division THE UNIVERSITY OF BRITISH COLUMBIA October,1957. ii - II. ABSTRACT The primary objective of this study was to establish the nature and extent of the changes with age in sucrase, maltase and lactase activity in the small intestine of the laboratory Wistar rat, raised on a basal diet. The author was, in addition, interested in the possibility of these changes being brought about by the presence or absence of certain specific dietary factors. Analysis have shown marked changes in the activities of these three enzymes with advancing age in Wistar rats weaned at 21 days on to a basal diet. Lactase activity was found to remain at a high level from 18 to 20 days during which time a sharp and uniform drop in activity was indicated. The extent of this drop was found to be great, approximately 80 per cent of the pre-weaned level. In contrast sucrase activity of the small intestine in the pre-weaned rat was negligible and underwent a sharp increase in activity at the weaning age of 21 days. Maltase activity in the pre-weaned Wistar rat was appreciable and was found to increase significantly at weaning. Early weaning at 15 days brought about an earlier decline in lactase activity and a corresponding early rise in sucrase and maltase activities. When early weaning was immedi• ately followed by the feeding of condensed milk no apparent maintenance of lactase activity was noted. Similarily when older rats, 28 days of age, were fed condensed milk no increase - iii - in lactase activity was apparent. Neither the condensed milk nor basal diets induced apparent differences on the effect of early weaning on sucrase and maltase activity. Apparent maintenance of lactase activity above those levels demonstrated in rats weaned at 21 days on to a basal diet was accomplished by fostering 16 day old rats on dams which had littered from four to five days prior to this transfer and which were assumed to be lactating at a somewhat greater rate than had the original mothers. It was noted however that this fostering process had no apparent influence on the extent of the changes in sucrase and maltase activities. The feeding of purified sugar diets containing two different levels of each of the three sugars, sucrose, maltose and lactose, had little effect on any of the three carbohydrases studied. Growth rates of the rats on these purified diets showed marked differences. The author suggests that the maintenance of lactase activity might be associated with the presence of an inductive component present in the milk of the freshly lactating dam, a component not necessarily present in the milk of the later period of lactation, and not necessarily a component of processed cow's milk. The absence of an adaptive lactase response to the feeding of lactose in this study and those of other workers suggest that lactose itself is unlikely this inducer. No adap• tive response to substrates could be demonstrated for either sucrase or maltase. In presenting this thesis in partial fulfilment of the requirements for an advanced degree at the University of British Columbia, I agree that the Library shall make it freely available for reference and study. I further agree that permission for extensive copying of this thesis for scholarly purposes may be granted by the Hea'el\of my Department or by his representative. It is understood that copying or publication of this thesis for// financial gain shall not be allowed without my written permission. ROBERT JOHN BOSE Department of THE nTVTRTnw on- awTMar. ^r.rjmr.v, The University of British Columbia, Vancouver 8, Canada. Date .TTTT.V jc\ 1957 I. ACKNOWLEDGEMENT The writer wishes to thank Dean Blythe Eagles, Chairman of the Division of Animal Science, for providing the facilities with which to conduct this experiment. Sincere appreciation is expressed to Dr. W. D. Kitts, Assistant Professor of Animal Husbandry, for sug• gesting this problem and for his direction, assistance and criticism during the course of this study. Thanks are expressed to Dr. A. J. Wood and to Dr. J. J. R. Campbell for their advice and criticisms. TABLE OP CONTENTS PAGE I. ACKNOWLEDGEMENT i II. ABSTRACT ii III. INTRODUCTION 1 IV. HISTORICAL 3 A. Sucrase 3 B. Maltase 5 C. Lactase 7 D. General 8 V. METHODS AND MATERIALS 15 A. Methods 15 1. Housing of the Experimental Animals.. 15 2. Sacrifice and Dissection of the Animals..... 15 3. The Storage of Tissue Samples 16 4. Preparation of the Tissue Homogenates 16 5. Moisture Determination 17 6. Nitrogen Determination 17 7. The Determination of Enzyme Activity 18 B. Materials 23 1. The Basal Diet 23 2. The Condensed Milk Diet 24 3. The Synthetic Diets .. 25 4. Copper Solution 26 5. Perric Sulfate Solution (According to Bertrand) 26 6. Potassium Permanganate Solution 26 7. Sugar Solutions 26 8. Buffer Solutions 27 VI. RESULTS AND DISCUSSION 28 A. Optima pH for Sucrase, Maltase and Lactase Activity 28 B. The H-ion Concentration of the Small Intestine of the Rat at Various Ages 31 C. The Relationship Between Homogenate Nitrogen Content and Enzyme Activity 34 TABLE OF CONTENTS (Continued) PAGE D. The Effect of Inanition on Sucrase, Maltase and Lactase Activity 37 E. Sucrase, Maltase and Lactase Activity From Birth to 72 Days of Age. in the Small Intestine of the Wistar Eat Weaned on to a Basal Diet at 21 Days 39 F. The Effect on Sucrase, Maltase and .. Lactase Activity of Early Weaning and the Feeding of Condensed Milk and a Basal Diet at Various Ages in the Laboratory Wistar Rat 49 G. The Effect on Sucrase, Maltase and Lactase Activity of the Small Intestine of the Young Wistar Rat of Prolonged Suckling on Foster Dams 57 H. The Effect on Sucrase, Maltase and Lactase Activity of Various Levels of the Three Sugars, Sucrose, Maltose and Lactose in a Purified Synthetic Diet .for the Laboratory Wistar Rat. VII. SUMMARY AND CONCLUSIONS 71 VIII. BIBLIOGRAPHY 74 Ill. INTRODUCTION Digestion in its broad sense refers to the mechanical and chemical degradation of complex dietary constituents to forms that are suitably prepared for the absorptive processes of the alimentary tract. The rate at which any animal "breaks down" its complex dietary is necessarily a function of many mechanical and chemical processes. The composition of a mammal's dietary changes markedly from birth to adult life. The young ingests almost exclusively its mother's milk, the mature or post weaned animal utilizes essentially none of this food for its dietary needs. In view of the many highly specific digestive mechanisms, it seems reasonable to conclude that accomodation for this changing dietary must necessarily be made for by associated changes in the digestive complex of the animal. A great number of investigators have described the numerous enzymes or ferments present in the various regions of the alimentary tract. Much work has been conducted regarding the digestibility of various dietary constituents for a wide group of species. There is however, only scanty information on the quantitative measurement of the digestive enzymes. In this investigation the three carbohydrases, sucrase ( <*-D-glucosidoinvertase), maltase ( oC-D-glucopyranosidase) and lactase (y3 -D-galactosidase) have been assayed quantitatively in the small intestine of the Wistar rat at various ages. In addition, experiments have been conducted to demonstrate the presence or absence of enzymatic adaptation to dietary changes in these three carbohydrases present in this digestive organ of the laboratory rat. The Wistar rat was employed in this experiment because of its rapid growth rate, genetic uniformity, low cost and its availability in large numbers. The practical applications arising from information regarding the nature of the changes in the digestive complex of the laboratory rat would be the extrapolation of these fundamental principles to the feeding of domestic animals such as the pig, sheep and ox. Inherent changes in the elaboration of lactase would necessitate the feeding of lactose at definite ages in a manner paralleling the production of this hydrolytic enzyme in the digestive tract. If the elaboration of digestive enzymes is largely controlled by the presence of their specific substrates in the ingesta the feeding of starch, for example, to young dairy calves could substitute for the more costly milk diet commonly fed these animals. IV. HISTORICAL A brief description of the three carbohydrases is felt appropriate as an introduction to the discussion of the literature. A. Sucrase; Sucrase has been known the longest of all the carbo• hydrases. In 1828 Dumas and Boullay (14) described the uptake of water during the fermentation of sucrose by yeast. Sucrase has been termed invertase, invertin and saccharase. Two types of invertase are described, a fructosidase attacking the fructose end, and a glucosidase attacking: the glucose end of the sucrose molecule (44). Both types are found in certain yeasts. The invertebrates and vertebrates possess the glucoinvertase exclusively. Sucrase is reported absent from the saliva and gastric secretions of mammals (31,7)• Its presence in the small intestine of the foetus and still-born has been reported by Keene et al (27) and Tachibana (45). Neuberg and Mandl (44) suggest that the elaboration of intestinal sucrase is inde• pendent on the presence of food in the intestinal tract.
Recommended publications
  • Disaccharidase Deficiencies
    J Clin Pathol: first published as 10.1136/jcp.s3-5.1.22 on 1 January 1971. Downloaded from J. clin. Path., 24, Suppl. (Roy. Coll. Path.), 5, 22-28 Disaccharidase deficiencies G. NEALE From the Department ofMedicine, Royal Postgraduate Medical School, Du Cane Road, London Up to 12 years ago the absorption of disaccharides capable of hydrolysing maltose, which may explain was a problem in physiology which attracted little why maltase deficiency is not found as an isolated attention and which appeared to be unrelated to the defect of the enterocyte. Isomaltase and sucrase problems of clinical medicine. Indeed, most text- appear to be distinct but linked entities, and hence books stated incorrectly that the disaccharides were they are absent together in the hereditary condition hydrolysed to monosaccharides in the lumen of the of sucrase-isomaltase deficiency (Dahlquist and small intestine despite the evidence of half a century Telenius, 1969). Lactase activity consists of at least before, which had suggested that they were digested two separate enzymes, one of which is not in the by the mucosal surface (Reid, 1901). The renewal of brush border but within the cell (Zoppi, Hadom, interest in the subject of disaccharide absorption Gitzelmann, Kistler, and Prader, 1966). The signifi- occurred after the description of congenital lactase cance of intracellular lactase activity is uncertain. It deficiency by Holzel, Schwarz, and Sutcliffe (1959) cannot play any part in the normal digestion of and of sucrase-isomaltase deficiency by Weijers, lactose which is a function of the brush border of the van de Kamer, Mossel, and Dicke (1960).
    [Show full text]
  • Is There Hidden Sugar in Your Drink?
    Is There Hidden Sugar in Your Drink? Anjali Shankar 9th Grade Moravian Academy Upper School June 5th, 2020 Motivation - I have a big passion for the medical field, showed by last year’s project. - Food labels and nutrition have caught my eye and are important when eating. How do glucose levels Research in different drinks change after adding Question an invertase enzyme? Given that the invertase enzyme breaks down sucrose, glucose levels will rise after adding the enzyme because the sucrose will convert to Hypothesis glucose and fructose. Coca Cola will have the most glucose because it has the most calories of each drink. Glucose - Chemical compound in the body - C6H12O6 - Comes from food and drink - Generally rich in sugars/carbohydrates - Used for many purposes: - Used to make energy (ATP) in cellular respiration - Stores energy - Used to build carbohydrates Chemical Reaction - A chemical reaction transfers a set of compounds into another - Reactants: Enter into a chemical reaction - Products: Compounds produced by the reaction - Catalyst: Speeds up the rate of a chemical reaction - Enzyme: Biological catalysts; usually proteins The formula for this experiment is: Invertase Sucrose + Water Glucose + Fructose Invertase C12H22O11 + H20 C6H12O6 + C6H12O6 In the Body - The most common sugar is eaten as sucrose. - Also known as table sugar - It is broken down in the body into glucose and fructose through a chemical reaction during digestion. - Fructose: Contains the same elements as glucose, but has a different chemical construction - Often used to make more glucose - The reaction is catalyzed by an enzyme named sucrase. - Modeled by invertase in experiment - The pancreas monitors blood sugar, or amount of glucose in the body.
    [Show full text]
  • Ep 2 246 408 A2
    (19) & (11) EP 2 246 408 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 03.11.2010 Bulletin 2010/44 C09K 8/60 (2006.01) (21) Application number: 10158819.2 (22) Date of filing: 13.11.2000 (84) Designated Contracting States: • Norman, Monica AT BE CH CY DE DK ES FI FR GB GR IE IT LI LU Houston, TX 77041 (US) MC NL PT • Symes, Kenneth C. Designated Extension States: Bradford, RO Yorkshire BD14 6LR (GB) • Mistry, Kishor K. (30) Priority: 12.11.1999 US 165393 P Keighley, East Moton, BD20 5UU (GB) (62) Document number(s) of the earlier application(s) in • Ballard, David A. accordance with Art. 76 EPC: Stonehaven, 00980356.0 / 1 232 329 Aberdeenshire AB39 3PQ (GB) (27) Previously filed application: (74) Representative: Hull, John Philip 13.11.2000 PCT/US03/01106 Beck Greener Fulwood House (71) Applicant: M-I L.L.C. 12 Fulwood Place Houston, TX 77072 (US) London WC1V 6HR (GB) (72) Inventors: Remarks: • Freeman, Michael A. This application was filed on 31-03-2010 as a Kingwood, TX 77345 (US) divisional application to the application mentioned • Jiang, Ping under INID code 62. 3400 Sandnes (NO) (54) Method and composition f or the triggered release of polymer-degrading agents for oil field use (57) Disclosed are methods and related composi- tions for altering the physical and chemical properties of a substrate used in hydrocarbon exploitation, such as in downhole drilling operations. In a preferred embodiment a method involves formulating a fluid, tailored to the spe- cific drilling conditions, that contains one or more inacti- vated enzymes.
    [Show full text]
  • 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.
    [Show full text]
  • Characterization of Substrate Binding and Catalytic Mechanisms of An
    Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 1988 Characterization of substrate binding and catalytic mechanisms of an endoxylanase, amylosucrase, and porcine pancreatic alpha-amylase Bernard Yi Tao Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Biochemistry Commons, and the Chemical Engineering Commons Recommended Citation Tao, Bernard Yi, "Characterization of substrate binding and catalytic mechanisms of an endoxylanase, amylosucrase, and porcine pancreatic alpha-amylase " (1988). Retrospective Theses and Dissertations. 8807. https://lib.dr.iastate.edu/rtd/8807 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. INFORMATION TO USERS The most advanced technology has been used to photo­ graph and reproduce this manuscript from the microfilm master, UMI films the original text directly fi'om the copy submitted. Thus, some dissertation copies are in typewriter face, while others may be from a computer printer. In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyrighted material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are re­ produced by sectioning the original, beginning at the upper left-hand comer and continuing from left to right in equal sections with small overlaps.
    [Show full text]
  • Production of Carbohydrases for Developing Soy Meal As
    PRODUCTION OF CARBOHYDRASES FOR DEVELOPING SOY MEAL AS PROTEIN SOURCE FOR ANIMAL FEED A Dissertation Presented to The Graduate Faculty of The University of Akron In Partial Fulfillment Of the Requirements for the Degree Doctor of Philosophy Qian Li May, 2017 PRODUCTION OF CARBOHYDRASES FOR DEVELOPING SOY MEAL AS PROTEIN SOURCE FOR ANIMAL FEED Qian Li Dissertation Approved: Accepted: Advisor Department Chair Dr. Lu-Kwang Ju Dr. Michael H. Cheung Committee Member Dean of the College Dr. Jie Zheng Dr. Donald P. Visco Jr. Committee Member Dean of the Graduate School Dr. Lingyun Liu Dr. Chand Midha Committee Member Date Dr. Ge Zhang Committee Member Dr. Pei-Yang Liu ii ABSTRACT Global demand for seafood is growing rapidly and more than 40% of the demand is met by aquaculture. Conventional aquaculture diet used fishmeal as the protein source. The limited production of fishmeal cannot meet the increase of aquaculture production. Therefore, it is desirable to partially or totally replace fishmeal with less-expensive protein sources, such as poultry by-product meal, feather meal blood meal, or meat and bone meal. However, these feeds are deficient in one or more of the essential amino acids, especially lysine, isoleucine and methionine. And, animal protein sources are increasingly less acceptable due to health concerns. One option is to utilize a sustainable, economic and safe plant protein sources, such as soybean. The soybean industry has been very prominent in many countries in the last 20 years. The worldwide soybean production has increased 106% since 1996 to 2010[1]. Soybean protein is becoming the best choice of sustainable, economic and safe protein sources.
    [Show full text]
  • Structures and Characteristics of Carbohydrates in Diets Fed to Pigs: a Review Diego M
    Navarro et al. Journal of Animal Science and Biotechnology (2019) 10:39 https://doi.org/10.1186/s40104-019-0345-6 REVIEW Open Access Structures and characteristics of carbohydrates in diets fed to pigs: a review Diego M. D. L. Navarro1, Jerubella J. Abelilla1 and Hans H. Stein1,2* Abstract The current paper reviews the content and variation of fiber fractions in feed ingredients commonly used in swine diets. Carbohydrates serve as the main source of energy in diets fed to pigs. Carbohydrates may be classified according to their degree of polymerization: monosaccharides, disaccharides, oligosaccharides, and polysaccharides. Digestible carbohydrates include sugars, digestible starch, and glycogen that may be digested by enzymes secreted in the gastrointestinal tract of the pig. Non-digestible carbohydrates, also known as fiber, may be fermented by microbial populations along the gastrointestinal tract to synthesize short-chain fatty acids that may be absorbed and metabolized by the pig. These non-digestible carbohydrates include two disaccharides, oligosaccharides, resistant starch, and non-starch polysaccharides. The concentration and structure of non-digestible carbohydrates in diets fed to pigs depend on the type of feed ingredients that are included in the mixed diet. Cellulose, arabinoxylans, and mixed linked β-(1,3) (1,4)-D-glucans are the main cell wall polysaccharides in cereal grains, but vary in proportion and structure depending on the grain and tissue within the grain. Cell walls of oilseeds, oilseed meals, and pulse crops contain cellulose, pectic polysaccharides, lignin, and xyloglucans. Pulse crops and legumes also contain significant quantities of galacto-oligosaccharides including raffinose, stachyose, and verbascose.
    [Show full text]
  • Purification, Characterization and Gene Analysis of a New Α-Glucosidase from Shiraia Sp
    Ann Microbiol (2017) 67:65–77 DOI 10.1007/s13213-016-1238-y ORIGINAL ARTICLE Purification, characterization and gene analysis of a new α-glucosidase from shiraia sp. SUPER-H168 Ruijie Gao1 & Huaxiang Deng1 & Zhengbing Guan1 & Xiangru Liao1 & Yujie Cai 1 Received: 21 October 2015 /Accepted: 19 October 2016 /Published online: 27 October 2016 # Springer-Verlag Berlin Heidelberg and the University of Milan 2016 Abstract A new α-glucosidase from Shiraia sp. SUPER- Keywords α-glucosidase . Characterization . Gene analysis . H168 under solid-state fermentation was purified by alcohol Purification . Shiraia sp. SUPER-H168 . Solid-state precipitation and anion-exchange and by gel filtration chro- fermentation matography. The optimum pH and temperature of the purified α-glucosidase were 4.5 and 60 °C, respectively, using p- nitrophenyl-α-glucopyranoside (α-pNPG) as a substrate. Introduction Ten millimoles of sodium dodecyl sulfate, Fe2+,Cu2+, and Ag+ reduced the enzyme activity to 0.7, 7.6, 26.0, and Glycoside hydrolases (EC 3.2.1.-) are a widespread group of 6.2 %, respectively, of that of the untreated enzyme. The enzymes that hydrolyze the glycosidic bond between two or Km, Vmax,andkcat/Km of the α-glucosidase were 0.52 mM, more carbohydrates or between a carbohydrate and a non- −1 4 −1 −1 3.76 U mg , and 1.3 × 10 Ls mol ,respectively.Km with carbohydrate moiety. α-glucosidases (EC 3.2.1.20, α-D- maltose was 0.62 mM. Transglycosylation activities were ob- glucoside glucohydrolase) constitute a group of exo-acting served with maltose and sucrose as substrates, while there was glycoside hydrolases of diverse specificities that catalyze the no transglycosylation with trehalose.
    [Show full text]
  • 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.
    [Show full text]
  • The Maltase-Glucoamylase Gene: Common Ancestry to Sucrase-Isomaltase with Complementary Starch Digestion Activities
    The maltase-glucoamylase gene: Common ancestry to sucrase-isomaltase with complementary starch digestion activities Buford L. Nichols*†, Stephen Avery*, Partha Sen*, Dallas M. Swallow‡, Dagmar Hahn§, and Erwin Sterchi§ *U.S. Department of Agriculture, Agricultural Research Service, Children’s Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine, Houston, TX 77030-2600; ‡Galton Laboratory, Department of Biology, University College London, Wolfson House, 4 Stephenson Way, London NW1 2HE, United Kingdom; and §Institute of Biochemistry and Molecular Biology, University of Bern, Buehlstrasse 28, CH-3012 Bern, Switzerland Communicated by John Waterlow, University of London, London, United Kingdom, December 4, 2002 (received for review April 17, 2002) Brush-border maltase-glucoamylase (MGA) activity serves as the ␣1-4 linkages (3, 4). ␣-Amylase bypasses the ␣1-6 linkages of final step of small intestinal digestion of linear regions of dietary amylopectin and thus produces branched maltose oligosaccha- starch to glucose. Brush-border sucrase-isomaltase (SI) activity is rides. Both families of maltose oligosaccharides are not absorb- complementary, through digestion of branched starch linkages. able without further processing to glucose by hydrolysis at the Here we report the cloning and sequencing of human MGA gene nonreducing ends of 1-4 and 1-6 oligomers (3). Two different and demonstrate its close evolutionary relationship to SI. The gene mammalian small intestinal mucosal brush border-anchored is Ϸ82,000 bp long and located at chromosome 7q34. Forty-eight enzymes, MGA and SI, carry out this hydrolysis to glucose (3). exons were identified. The 5؅ gene product, when expressed as the Enzyme substrate specificities of human SI complement those of N-terminal protein sequence, hydrolyzes maltose and starch, but MGA.
    [Show full text]
  • WO 2009/152285 Al
    (12) INTERNATIONALAPPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date 17 December 2009 (17.12.2009) WO 2009/152285 Al (51) International Patent Classification: CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, DO, C12N 15/82 (2006.01) DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, (21) International Application Number: KR, KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, PCT/US2009/046968 ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, (22) International Filing Date: NO, NZ, OM, PE, PG, PH, PL, PT, RO, RS, RU, SC, SD, 11 June 2009 ( 11.06.2009) SE, SG, SK, SL, SM, ST, SV, SY, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. (25) Filing Language: English (84) Designated States (unless otherwise indicated, for every (26) Publication Language: English kind of regional protection available): ARIPO (BW, GH, (30) Priority Data: GM, KE, LS, MW, MZ, NA, SD, SL, SZ, TZ, UG, ZM, 61/060,789 11 June 2008 ( 11.06.2008) US ZW), Eurasian (AM, AZ, BY, KG, KZ, MD, RU, TJ, TM), European (AT, BE, BG, CH, CY, CZ, DE, DK, EE, (71) Applicant (for all designated States except US): SYN- ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, LV, GENTA PARTICIPATIONS AG [CH/CH]; 4058 MC, MK, MT, NL, NO, PL, PT, RO, SE, SI, SK, TR), Schwarzwaldallee 215, CH-4058 Basel (CH).
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2011/0165635 A1 Copenhaver Et Al
    US 2011 O165635A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2011/0165635 A1 Copenhaver et al. (43) Pub. Date: Jul. 7, 2011 (54) METHODS AND MATERALS FOR Publication Classification PROCESSINGA FEEDSTOCK (51) Int. Cl. CI2P I 7/04 (2006.01) (75) Inventors: Gregory P. Copenhaver, Chapel CI2P I/00 (2006.01) Hill, NC (US); Daphne Preuss, CI2P 7/04 (2006.01) Chicago, IL (US); Jennifer Mach, CI2P 7/16 (2006.01) Chicago, IL (US) CI2P 7/06 (2006.01) CI2P 5/00 (2006.01) CI2P 5/02 (2006.01) (73) Assignee: CHROMATIN, INC., Chicago, IL CI2P3/00 (2006.01) (US) CI2P I/02 (2006.01) CI2N 5/10 (2006.01) (21) Appl. No.: 12/989,038 CI2N L/15 (2006.01) CI2N I/3 (2006.01) (52) U.S. Cl. ........... 435/126; 435/41; 435/157; 435/160; (22) PCT Fled: Apr. 21, 2009 435/161; 435/166; 435/167; 435/168; 435/171; 435/419,435/254.11: 435/257.2 (86) PCT NO.: PCT/US2O09/041260 (57) ABSTRACT S371 (c)(1), The present disclosure relates generally to methods for pro (2), (4) Date: Mar. 11, 2011 cessing a feedstock. Specifically, methods are provided for processing a feedstock by mixing the feedstock with an addi tive organism that comprises one or more transgenes coding Related U.S. Application Data for one or more enzymes. The expressed enzymes may be (60) Provisional application No. 61/046,705, filed on Apr. capable of breaking down cellulosic and lignocellulosic 21, 2008. materials and converting them to a biofuel.
    [Show full text]