Enzymes at Work
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
Enzymes Handling/Processing
Enzymes Handling/Processing 1 Identification of Petitioned Substance 2 3 This Technical Report addresses enzymes used in used in food processing (handling), which are 4 traditionally derived from various biological sources that include microorganisms (i.e., fungi and 5 bacteria), plants, and animals. Approximately 19 enzyme types are used in organic food processing, from 6 at least 72 different sources (e.g., strains of bacteria) (ETA, 2004). In this Technical Report, information is 7 provided about animal, microbial, and plant-derived enzymes generally, and more detailed information 8 is presented for at least one model enzyme in each group. 9 10 Enzymes Derived from Animal Sources: 11 Commonly used animal-derived enzymes include animal lipase, bovine liver catalase, egg white 12 lysozyme, pancreatin, pepsin, rennet, and trypsin. The model enzyme is rennet. Additional details are 13 also provided for egg white lysozyme. 14 15 Chemical Name: Trade Name: 16 Rennet (animal-derived) Rennet 17 18 Other Names: CAS Number: 19 Bovine rennet 9001-98-3 20 Rennin 25 21 Chymosin 26 Other Codes: 22 Prorennin 27 Enzyme Commission number: 3.4.23.4 23 Rennase 28 24 29 30 31 Chemical Name: CAS Number: 32 Peptidoglycan N-acetylmuramoylhydrolase 9001-63-2 33 34 Other Name: Other Codes: 35 Muramidase Enzyme Commission number: 3.2.1.17 36 37 Trade Name: 38 Egg white lysozyme 39 40 Enzymes Derived from Plant Sources: 41 Commonly used plant-derived enzymes include bromelain, papain, chinitase, plant-derived phytases, and 42 ficin. The model enzyme is bromelain. -
• Glycolysis • Gluconeogenesis • Glycogen Synthesis
Carbohydrate Metabolism! Wichit Suthammarak – Department of Biochemistry, Faculty of Medicine Siriraj Hospital – Aug 1st and 4th, 2014! • Glycolysis • Gluconeogenesis • Glycogen synthesis • Glycogenolysis • Pentose phosphate pathway • Metabolism of other hexoses Carbohydrate Digestion! Digestive enzymes! Polysaccharides/complex carbohydrates Salivary glands Amylase Pancreas Oligosaccharides/dextrins Dextrinase Membrane-bound Microvilli Brush border Maltose Sucrose Lactose Maltase Sucrase Lactase ‘Disaccharidase’ 2 glucose 1 glucose 1 glucose 1 fructose 1 galactose Lactose Intolerance! Cause & Pathophysiology! Normal lactose digestion Lactose intolerance Lactose Lactose Lactose Glucose Small Intestine Lactase lactase X Galactose Bacteria 1 glucose Large Fermentation 1 galactose Intestine gases, organic acid, Normal stools osmotically Lactase deficiency! active molecules • Primary lactase deficiency: อาการ! genetic defect, การสราง lactase ลด ลงเมออายมากขน, พบมากทสด! ปวดทอง, ถายเหลว, คลนไสอาเจยนภาย • Secondary lactase deficiency: หลงจากรบประทานอาหารทม lactose acquired/transient เชน small bowel เปนปรมาณมาก เชนนม! injury, gastroenteritis, inflammatory bowel disease! Absorption of Hexoses! Site: duodenum! Intestinal lumen Enterocytes Membrane Transporter! Blood SGLT1: sodium-glucose transporter Na+" Na+" •! Presents at the apical membrane ! of enterocytes! SGLT1 Glucose" Glucose" •! Co-transports Na+ and glucose/! Galactose" Galactose" galactose! GLUT2 Fructose" Fructose" GLUT5 GLUT5 •! Transports fructose from the ! intestinal lumen into enterocytes! -
Revision of Ecolabel Criteria for Laundry Detergents 2008-2010
European Ecolabel ENV.G.2/SER2007/0073rl Commission Decision of 28 April 2011 Revision of Ecolabel Criteria for Laundry Detergents 2008-2010 Background report Prepared by Ecolabelling Denmark This document was last updated February 2011 INDEX 1. SUMMARY ....................................................................... 2 2. MARKET REVIEW ............................................................. 4 2.1. EUROPEAN MARKET FOR LAUNDRY DETERGENTS AND ADDITIVES .................................... 4 2.1.1. Laundry detergents .............................................................................................. 4 2.1.2. Fabric softeners ..................................................................................................... 5 2.1.3. Stain Removers ...................................................................................................... 6 2.2. WASHING HABITS IN EUROPE ............................................................................................. 6 2.3. ECOLABEL LICENSES AND PRODUCTS TODAY ..................................................................... 6 3. PRODUCT GROUP DEFINITION ........................................ 8 4. INTRODUCTION TO REVISED ECOLABEL CRITERIA ....... 10 5. REVISED ECOLABEL CRITERIA ...................................... 13 5.1. REVISED CRITERIA ............................................................................................................. 13 5.1.1. General remarks ................................................................................................. -
Updating the Sequence-Based Classification of Glycosyl Hydrolases
Article Updating the sequence-based classification of glycosyl hydrolases HENRISSAT, Bernard, BAIROCH, Amos Marc Reference HENRISSAT, Bernard, BAIROCH, Amos Marc. Updating the sequence-based classification of glycosyl hydrolases. Biochemical Journal, 1996, vol. 316 ( Pt 2), p. 695-6 PMID : 8687420 DOI : 10.1042/bj3160695 Available at: http://archive-ouverte.unige.ch/unige:36909 Disclaimer: layout of this document may differ from the published version. 1 / 1 Biochem. J. (1996) 316, 695–696 (Printed in Great Britain) 695 BIOCHEMICAL JOURNAL Updating the sequence-based classification of available. When the number of glycosyl hydrolase sequences reached C 480, ten additional families (designated 36–45) could glycosyl hydrolases be defined and were added to the classification [2]. There are at present over 950 sequences of glycosyl hydrolases in the data- A classification of glycosyl hydrolases based on amino-acid- banks (EMBL}GenBank and SWISS-PROT). Their analysis sequence similarities was proposed in this Journal a few years shows that the vast majority of the C 470 additional sequences ago [1]. This classification originated from the analysis of C 300 that have become available since the last update could be classified sequences and their grouping into 35 families designated 1–35. in the existing families. However, several sequences not fitting Because such a classification is necessarily sensitive to the sample, the existing families allow the definition of new families (desig- it was anticipated that it was incomplete and that new families nated 46–57) (Table 1). When the several present genome would be determined when additional sequences would become sequencing projects have reached completion, the number of Table 1 New families in the classification of glycosyl hydrolases Family Enzyme Organism SWISS-PROT EMBL/GenBank 46 Chitosanase Bacillus circulans MH-K1 P33673 D10624 46 Chitosanase Streptomyces sp. -
ATP-Citrate Lyase Has an Essential Role in Cytosolic Acetyl-Coa Production in Arabidopsis Beth Leann Fatland Iowa State University
Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 2002 ATP-citrate lyase has an essential role in cytosolic acetyl-CoA production in Arabidopsis Beth LeAnn Fatland Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Molecular Biology Commons, and the Plant Sciences Commons Recommended Citation Fatland, Beth LeAnn, "ATP-citrate lyase has an essential role in cytosolic acetyl-CoA production in Arabidopsis " (2002). Retrospective Theses and Dissertations. 1218. https://lib.dr.iastate.edu/rtd/1218 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]. ATP-citrate lyase has an essential role in cytosolic acetyl-CoA production in Arabidopsis by Beth LeAnn Fatland A dissertation submitted to the graduate faculty in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY Major: Plant Physiology Program of Study Committee: Eve Syrkin Wurtele (Major Professor) James Colbert Harry Homer Basil Nikolau Martin Spalding Iowa State University Ames, Iowa 2002 UMI Number: 3158393 INFORMATION TO USERS The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleed-through, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send a complete manuscript and there are missing pages, these will be noted. -
Risk Assessment Guidance for Enzyme-Containing Products
Risk Assessment Guidance for Enzyme-Containing Products The Soap and Detergent Association Table of Contents Preface 2 Executive Summary 3 Chapter 1 — Introduction to Enzymes 4 Chapter 2 — Introduction to Risk Assessment 6 Chapter 3 — Hazard Identification 8 Chapter 4 — Dose-Response Assessment 11 Chapter 5 — Exposure Assessment 17 Chapter 6 — Risk Characterization 23 Chapter 7 — Risk Management 28 Chapter 8 — Conclusions 30 Bibliography 31 Glossary 38 Appendix 1 — Estimation of Exposure to Enzymes from Early Detergent Formulations 41 Appendix 2 — Enzyme Risk Assessments of Hand-Laundering Practices 51 Appendix 3 — Spray Pre-Treater Case Study 54 FIGURES — 1, 2, 3 A, 3 B, 4 TABLE — 1 Copyright © 2005:The Soap and Detergent Association. Al rights reserved. No part of this document may be reproduced or transmitted in any form or by any means, electronic or mechanical, including photocopying, recording, or by any infor- mation storage retrieval system, without written permission from the publisher. For information, contact:The Soap and Detergent Association, 1500 K Street, NW, Suite 300,Washington, DC 20005, USA. Telephone: +1-202-347-2900. Fax: +1-202-347-4110. Email: [email protected]. Web: www.sdahq.org PREFACE he laundry product industry has implemented For additional information on risk assessment and Ta successful product stewardship program to risk practices for enzymes, contact your enzyme promote the safe use of enzymes in the workplace supplier, or and by users of their products,using both appropriate risk assessment and risk management practices. The Soap and Detergent Association Much of the information about enzymes for laundry 1500 K Street, NW, Suite 300 applications can be applied to other finished products Washington, DC 20005 including those in the cleaning and personal care Tel: 202-347-2900 markets. -
Cellulases: Characteristics, Sources, Production, and Applications
8 CELLULASES: CHARACTERISTICS, SOURCES, PRODUCTION, AND APPLICATIONS Xiao-Zhou Zhang and Yi-Heng Percival Zhang 8.1 INTRODUCTION lulases: (1) endoglucanases (EC 3.2.1.4), (2) exogluca- nases, including cellobiohydrolases (CBHs) (EC Cellulose is the most abundant renewable biological 3.2.1.91), and (3) β -glucosidase (BG) (EC 3.2.1.21). To resource and a low-cost energy source based on energy hydrolyze and metabolize insoluble cellulose, the micro- content ($3–4/GJ) ( Lynd et al., 2008 ; Zhang, 2009 ). The organisms must secrete the cellulases (possibly except production of bio-based products and bioenergy from BG) that are either free or cell-surface-bound. Cellu- less costly renewable lignocellulosic materials would lases are increasingly being used for a large variety of bring benefi ts to the local economy, environment, and industrial purposes—in the textile industry, pulp and national energy security ( Zhang, 2008 ). paper industry, and food industry, as well as an additive High costs of cellulases are one of the largest obsta- in detergents and improving digestibility of animal cles for commercialization of biomass biorefi neries feeds. Now cellulases account for a signifi cant share of because a large amount of cellulase is consumed for the world ’ s industrial enzyme market. The growing con- biomass saccharifi cation, for example, ∼ 100 g enzymes cerns about depletion of crude oil and the emissions of per gallon of cellulosic ethanol produced ( Zhang et al., greenhouse gases have motivated the production of bio- 2006b ; Zhu et al., 2009 ). In order to decrease cellulase ethanol from lignocellulose, especially through enzy- use, increase volumetric productivity, and reduce capital matic hydrolysis of lignocelluloses materials—sugar investment, consolidated bioprocessing ( CBP ) has been platform ( Bayer et al., 2007 ; Himmel et al., 1999 ; Zaldi- proposed by integrating cellulase production, cellulose var et al., 2001 ). -
Generated by SRI International Pathway Tools Version 25.0, Authors S
An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Gcf_000238675-HmpCyc: Bacillus smithii 7_3_47FAA Cellular Overview Connections between pathways are omitted for legibility. -
United States Patent (19) 11 Patent Number: 5,981,835 Austin-Phillips Et Al
USOO598.1835A United States Patent (19) 11 Patent Number: 5,981,835 Austin-Phillips et al. (45) Date of Patent: Nov. 9, 1999 54) TRANSGENIC PLANTS AS AN Brown and Atanassov (1985), Role of genetic background in ALTERNATIVE SOURCE OF Somatic embryogenesis in Medicago. Plant Cell Tissue LIGNOCELLULOSC-DEGRADING Organ Culture 4:107-114. ENZYMES Carrer et al. (1993), Kanamycin resistance as a Selectable marker for plastid transformation in tobacco. Mol. Gen. 75 Inventors: Sandra Austin-Phillips; Richard R. Genet. 241:49-56. Burgess, both of Madison; Thomas L. Castillo et al. (1994), Rapid production of fertile transgenic German, Hollandale; Thomas plants of Rye. Bio/Technology 12:1366–1371. Ziegelhoffer, Madison, all of Wis. Comai et al. (1990), Novel and useful properties of a chimeric plant promoter combining CaMV 35S and MAS 73 Assignee: Wisconsin Alumni Research elements. Plant Mol. Biol. 15:373-381. Foundation, Madison, Wis. Coughlan, M.P. (1988), Staining Techniques for the Detec tion of the Individual Components of Cellulolytic Enzyme 21 Appl. No.: 08/883,495 Systems. Methods in Enzymology 160:135-144. de Castro Silva Filho et al. (1996), Mitochondrial and 22 Filed: Jun. 26, 1997 chloroplast targeting Sequences in tandem modify protein import specificity in plant organelles. Plant Mol. Biol. Related U.S. Application Data 30:769-78O. 60 Provisional application No. 60/028,718, Oct. 17, 1996. Divne et al. (1994), The three-dimensional crystal structure 51 Int. Cl. ............................. C12N 15/82; C12N 5/04; of the catalytic core of cellobiohydrolase I from Tricho AO1H 5/00 derma reesei. Science 265:524-528. -
Use of Plackett-Burman Design for Rapid Screening of Diverse Raw Pectin Sources for Cold-Active Polygalacturonase and Amylase Production by Geotrichum Sp
Int.J.Curr.Microbiol.App.Sci (2015) 4(6): 821-827 ISSN: 2319-7706 Volume 4 Number 6 (2015) pp. 821-827 http://www.ijcmas.com Original Research Article Use of Plackett-Burman Design for rapid Screening of Diverse Raw Pectin Sources for Cold-Active Polygalacturonase and Amylase Production by Geotrichum sp K. Divya and P. Naga Padma* Bhavan s Vivekananda College of Science, Humanities and Commerce, Secunderabad 94, India *Corresponding author A B S T R A C T Cold active polygalacturonases and amylases play significant role in extraction and clarification of fruit juices at industrial level. An optimized production medium with low cost substrates would be very useful for commercial production of these enzymes. The present study was done to screen low cost pectin and starch K e y w o r d s substrates for cold active enzymes production. The different pectin and starch sources screened were fruit and vegetables peels like citrus, pineapple, apple, Amylase, banana, mango, guava, carrot, beetroot, bottle gourd, ridge gourd and potato. For Cold-active efficient screening of the best sources a statistical design like Plackett-Burman was enzyme, used as in this design n variables can be studied in just n-1 experiments only. A Geotrichum sps, twelve experimental design Plackett-Burman was used as the best sources can be Poly shortlisted in consideration with their interactive effects. The pectinolytic and galacturonase, amylolytic yeast isolate was identified as Geotrichum sps and was used for the Plackett- present study. Cold-active pectinase and amylase enzyme activity was assayed by Burman, dinitrosalicylic acid (DNS) method. -
Functional Assignments in the Enolase Superfamily: Investigations of Two Divergent Groups of D-Galacturonate Dehydratases and Galactarate Dehydratase-Iii
FUNCTIONAL ASSIGNMENTS IN THE ENOLASE SUPERFAMILY: INVESTIGATIONS OF TWO DIVERGENT GROUPS OF D-GALACTURONATE DEHYDRATASES AND GALACTARATE DEHYDRATASE-III BY FIONA PATRICIA GRONINGER-POE i DISSERTATION Submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biochemistry in the Graduate College of the University of Illinois at Urbana-Champaign, 2014 Urbana, Illinois Doctoral Committee: Professor John A. Gerlt, Chair Professor John E. Cronan, Jr. Associate Professor Rutilo Fratti Associate Professor Raven H. Huang ABSTRACT More than a decade after the genomic age, full genome sequencing is cost-effective and fast, allowing for the deposit of an ever increasing number of DNA sequences. New fields have arisen from this availability of genomic information, and the way we think about biochemistry and enzymology has been transformed. Unfortunately, there is no robust method for accurately determining the functions of enzymes encoded by these sequences that matches the speed in which genomes are deposited into public databases. Functional assignment of enzymes remains of utmost importance in understanding microbial metabolism and has applications in agriculture by examining bacterial plant pathogen metabolism and additionally in human health by providing metabolic context to the human gut microbiome. To aid in the functional identification of proteins, enzymes can be grouped into superfamilies which share common structural motifs as well as mechanistic features. To this end, the enolase superfamily is an excellent model system for functional assignment because more than half of the members still lack functional identification. Structurally, these enzymes contain substrate specificity residues in the N-terminal capping domain and catalytic residues in the C-terminal barrel domain. -
Cells of Commelina Communis1 Received for Publication April 8, 1987 and in Revised Form June 13, 1987 NINA L
Plant Physiol. (1987) 85, 360-364 0032-0889/87/85/0360/05/$01.00/0 Localization of Carbohydrate Metabolizing Enzymes in Guard Cells of Commelina communis1 Received for publication April 8, 1987 and in revised form June 13, 1987 NINA L. ROBINSON2 AND JACK PREISS*3 Department ofBiochemistry and Biophysics, University ofCalifornia, Davis, California 95616 ABSTRACI leaves. The sucrose is either degraded in the apoplast or in the cytoplasm of the storage cell. Sucrose, or its degradation prod- The lliztion ofenzymes involved in the flow of carbon into and out ucts, can be further metabolized to the triose-P or 3-PGA level. of starch was determined in guard cells of Commelina communis. The These compounds may then move into the amyloplast via the guard cell chloroplasts were separated from the rest of the cellular triose-P/Pi translocator and are converted into starch. However, components by a modification of published microfuge methods. The at present, the presence of the triose-P/Pi translocator in amy- enzymes of interest were then assayed in the supernatant and chloroplast loplasts has not been demonstrated. Assuming that the triose-P/ fractions. The chloroplast yield averaged 75% with 10% cytoplasmic Pi translocator is present, the movement of carbon into starch contamination. The enzymes involved in starch biosynthesis, ADPglucose would be a reversal of the enzymic steps occurring in the cyto- pyrophosphorylase, starch synthase, and branching enzyme, are located plasm with the last several steps resulting in the direct incorpo- exclusively in the chloroplast fraction. The enzymes involved in starch ration of carbon into starch.