DOCSLIB.ORG

Exposure, Sensitization and Allergy to Industrial Enzymes

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Exposure, Sensitization and Allergy to Industrial Enzymes EXPOSURE, SENSITIZATION AND ALLERGY TO INDUSTRIAL ENZYMES Markku Vanhanen People and Work Research Reports 46 Finnish Institute of Occupational Health Department of Pulmology, Helsinki University Central Hospital Helsinki 2001 1 Cover Design Susanna Virtanen Layout Vammalan Kirjapaino Oy ISBN 951-802-453-7 ISSN 1237-6183 Vammalan Kirjapaino Oy Vammala 2001 2 To Sanna-Leena, Ilkka, Sini and Jukka 3 CONTENTS SUMMARY .................................................................................... 6 ACKNOWLEDGEMENTS ............................................................... 8 ABBREVIATIONS ........................................................................... 9 LIST OF ORIGINAL PUBLICATIONS .............................................. 10 1. INTRODUCTION ....................................................................... 11 2. REVIEW OF THE LITERATURE ................................................. 12 2.1. What enzymes are............................................................. 12 2.2. History of enzyme use and technology ............................. 12 2.3. Modern production of enzymes by microbes .................... 13 2.4. Classification of enzymes .................................................. 13 2.5. Applications of industrial enzymes .................................... 14 2.6. Health effects of industrial enzymes ................................. 17 2.6.1. Respiratory allergies caused by enzymes ................ 17 2.6.1.1. Detergent industry .................................. 17 2.6.1.2. Pharmaceutical industry, health care and related occupations ................................ 18 2.6.1.3. Baking industry ....................................... 19 2.6.1.4. Enzyme-producing industry ..................... 20 2.6.1.5. Other industries....................................... 21 2.6.2. Dermatitis due to enzymes .................................... 21 2.6.3. Allergy to enzymes among consumers................... 21 2.6.4. Determinants of sensitization ................................ 28 2.7. Characterization of enzyme allergens ............................... 29 2.8. Diagnosing enzyme-induced asthma with a challenge test 29 2.9. Monitoring of enzymes in the workplace air ..................... 30 2.9.1. Catalytic methods .................................................. 30 2.9.2. Immunologic methods ........................................... 34 2.10. Exposure guidelines for enzymes ...................................... 35 3. AIMS OF THE STUDY............................................................... 40 4. MATERIAL AND METHODS .................................................... 41 4.1. Workplaces and subjects ................................................... 41 4.2. Total dust and enzyme measurements .............................. 43 4 4.2.1. Sampling ................................................................ 43 4.2.2. Analysis .................................................................. 44 4.3. Assessment of work-related symptoms ............................. 44 4.4. Assessment of sensitization............................................... 45 4.4.1. Skin prick test ........................................................ 45 4.4.2. Immunoglobulin E measurements.......................... 46 4.5. Characterization of enzyme allergens ............................... 46 4.6. Lung function tests and testing bronchial hyperreactivity (study V)............................................................................ 46 4.7. Specific challenge tests (study V)....................................... 46 4.8. Statistical methods ............................................................ 47 5. RESULTS ................................................................................... 48 5.1. Enzyme and total dust measurements (studies I–IV).......... 48 5.2. Sensitization to enzymes (studies I–IV) .............................. 50 5.3. Sensitization to flours and storage mites .......................... 51 5.4. Sensitization to environmental allergens ........................... 51 5.5. Relation of atopy and smoking to sensitization to enzymes, flours and storage mites ................................................... 51 5.6. Work-related symptoms .................................................... 56 5.7. Specific challenge tests (study V)....................................... 57 5.8. Characterization of enzyme allergens ............................... 58 6. DISCUSSION ............................................................................. 61 6.1. Air concentration of dust and enzymes............................. 61 6.1.1. Total dust ............................................................... 61 6.1.2. Enzymes ................................................................. 62 6.2. Sensitization and allergy to enzymes................................. 65 6.3. Role of atopy in the sensitization to enzymes ................... 67 6.4. Diagnosing enzyme-induced asthma using specific bron- chial provocation test........................................................ 68 6.5. Characterization of enzyme allergens ............................... 69 6.6. Validity issues .................................................................... 69 6.6.1. Study design and selection of study populations ..... 69 6.6.2. Validity of the methods ......................................... 70 6.6.2.1. Assessment of sensitization..................... 70 6.6.2.2. Assessment of symptoms ........................ 70 6.6.2.3. Assessment of exposure .......................... 71 6.7. Prevention of allergies to enzymes .................................... 71 7. CONCLUSIONS ......................................................................... 74 8. REFERENCES ............................................................................. 76 ORIGINAL PUBLICATIONS (I–V) ................................................... 87 5 SUMMARY The production and use of industrial enzymes have increased markedly during the last few decades. Today, enzymes are used, for example, in the detergent, food, feed, textile and pulp and paper industries. Respiratory allergies to powdered microbial enzymes surfaced in the late 1960s in the detergent industry. With improvements in industrial hygiene, the problem abated. Since the 1980s, allergies have emerged in other industries however, notably in bakeries. A series of studies on enzyme allergy was performed in 1992–1997. The aim was to assess exposure and allergy to enzymes in Finnish enzyme manufacturing and industries using enzymes. Investigations were performed in four bakeries, one flour mill, one rye crisp factory, one detergent factory, four animal feed factories, one biotechnical research laboratory and one biotechnical plant having both research and production units. For determining α-amylase, a catalytic method was used which detects also the inherent amylase of flour. For protease detection both a catalytic method and a more specific immunologic procedure were used. Cellulase and xylanase were measured with an immunologic method. Powdered enzyme-containing additives were used in the bakeries, where high α-amylase levels, up to 6.6 µg/m3, were found during dough making. In other locations, the levels were generally lower, below 0.2 µg/m3. In addition, xylanase concentrations of 2– 200 ng/m3 (mean 65 ng/m3) were found, possibly also due to inherent xylanase. Enzyme-containing additives were mixed in the four mill, and α-amylase concentrations up to 1.1 µg/m3 and cellulase concentrations up to 180 ng/m3 were determined at the mixing sites. In the rye crisp factory the α-amylase levels were lower than in the bakeries (mean value 0.1 µg/m3 for personal samples and 0.03 µg/m3 for stationary samples). The cellulase concentrations ranged from 25 to 160 ng/m3 in different phases of the mixing, dough making and bread forming. At the same sites, lower levels (7– 40 ng/m3) of xylanase were measured. In the animal feed factories, the nonspecific assay showed high levels of protease (up to 0.4–2.9 µg/m3) and α-amylase (up to 0.2 µg/m3), which coincided with the high total dust levels but not with the amount of added enzyme. In the detergent factory, the protease levels, measured with a catalytic method, were generally below 50 ng/m3, but at the enzyme mixing site very high concentrations, above 1000 ng/m3, were found. The analysis with an immunologic method gave results of the same 6 order, indicating that the main origin of the protease was the added enzyme. Few measurements prior this study from the enzyme manufacturing industry had indicated cellulase concentrations on the order of 50 ng/m3 in laboratory work. Judging from job descriptions, much higher enzyme concentrations probably occurred occasionally during the mixing, drying and packing of enzymes. The prevalence of sensitization to enzymes, assessed by skin prick testing, was 7.8% in the bakeries, 4.8% in the flour mill and 2.7% in the rye crisp factory. When the office personnel was excluded, the figures were 8.4%, 5.3% and 3%, respectively. In the animal feed industry the corresponding prevalences were 4.6% and 7.1%, and in the detergent industry 11.8% and 22.5%. In the biotechnical research laboratory 11.7% of the workers and in the biotechnical plant 12.6% of the workers were sensitized. In the category of research, laboratory and enzyme manufacturing work, the rates were 12.6% and 15.4%, respectively. A statistically significant exposure-response linear trend was demonstrated among the biotechnical workers.
Load more

Recommended publications
  • 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 .................................................................................................
    [Show full text]
  • 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.
    [Show full text]
  • Application of Plant Proteolytic Enzymes for Tenderization of Rabbit Meat
    Biotechnology in Animal Husbandry 34 (2), p 229-238 , 2018 ISSN 1450-9156 Publisher: Institute for Animal Husbandry, Belgrade-Zemun UDC 637.5.039'637.55'712 https://doi.org/10.2298/BAH1802229D APPLICATION OF PLANT PROTEOLYTIC ENZYMES FOR TENDERIZATION OF RABBIT MEAT Maria Doneva, Iliana Nacheva, Svetla Dyankova, Petya Metodieva, Daniela Miteva Institute of Cryobiology and Food Technology, Cherni Vrah 53, 1407, Sofia, Bulgaria Corresponding author: Maria Doneva, e-mail: [email protected] Original scientific paper Abstract: The purpose of this study is to assess the tenderizing effect of plant proteolytic enzymes upon raw rabbit meat. Tests are performed on rabbit meat samples treated with papain and two vegetal sources of natural proteases (extracts of kiwifruit and ginger root). Two variants of marinade solutions are prepared from each vegetable raw materials– 50% (w/w) and 100 % (w/w), with a duration of processing 2h, 24h, and 48h. Changes in the following physico- chemical characteristics of meat have been observed: pH, water-holding capacity, cooking losses and quantity of free amino acids. Differences in values of these characteristics have been observed, both between control and test samples, as well as depending of treatment duration. For meat samples marinated with papain and ginger extracts, the water-holding capacity reached to 6.74 ± 0.04 % (papain), 5.58 ± 0.09 % (variant 1) and 6.80 ± 0.11 % (variant 2) after 48 hours treatment. In rabbit meat marinated with kiwifruit extracts, a significant increase in WHC was observed at 48 hours, 3.37 ± 0.07 (variant 3) and 6.84 ± 0.11 (variant 4).
    [Show full text]
  • Risk of Enzyme Allergy in the Detergent Industry
    Occup Environ Med 2000;57:121–125 121 Occup Environ Med: first published as 10.1136/oem.57.2.121 on 1 February 2000. Downloaded from Risk of enzyme allergy in the detergent industry Markku Vanhanen, Timo Tuomi, Ulla Tiikkainen, Outi Tupasela, Risto Voutilainen, Henrik Nordman Abstract sation to enzymes and the levels of exposure to Objectives—To assess the prevalence of protease in a detergent factory. enzyme sensitisation in the detergent industry. Material and methods Methods—A cross sectional study was DETERGENT FACTORY conducted in a detergent factory. Sensiti- The study was carried out in a factory produc- sation to enzymes was examined by skin ing laundry detergents and automatic dish prick and radioallergosorbent (RAST) washing detergents. The factory had been tests. 76 Workers were tested; 40 in manu- operating since the 1960s. New facilities were facturing, packing, and maintenance, and built in the mid-1980s. Detergents for laundry 36 non-exposed people in management and dish washing were produced in separate and sales departments. The workers were departments. The manufacturing of laundry interviewed for work related respiratory detergents includes mixing of raw materials and skin symptoms. Total dust concentra- with water and subsequent spray drying of the tions were measured by a gravimetric slurry, followed by addition of heat labile com- method, and the concentration of protease ponents such as enzymes. The addition of in air by a catalytic method. enzyme to the hopper took place manually a Results—Nine workers (22%) were sensi- few times in a shift. Further mixing to the tised to enzymes in the exposed group of detergent was automated.
    [Show full text]
  • Assessing the Risk of Type 1 Allergy to Enzymes Present in Laundry and Cleaning Products: Evidence from the Clinical Data
    Toxicology 271 (2010) 87–93 Contents lists available at ScienceDirect Toxicology journal homepage: www.elsevier.com/locate/toxicol Assessing the risk of type 1 allergy to enzymes present in laundry and cleaning products: Evidence from the clinical data Katherine Sarlo a,∗, Donald B. Kirchner a, Esperanza Troyano a, Larry A. Smith a, Gregory J. Carr a, Carlos Rodriguez b a The Procter & Gamble Company, Cincinnati, OH, United States b The Procter & Gamble Company, Brussels, Belgium article info abstract Article history: Microbial enzymes have been used in laundry detergent products for several decades. These enzymes Received 25 January 2010 have also long been known to have the potential to give rise to occupational type 1 allergic responses. A Received in revised form 22 February 2010 few cases of allergy among consumers using dusty enzyme detergents were reported in the early 1970s. Accepted 3 March 2010 Encapsulation of the enzymes along with other formula changes were made to ensure that consumer Available online 17 March 2010 exposure levels were sufficiently low that the likelihood of either the induction of IgE antibody (sensitiza- tion) or the elicitation of clinical symptoms be highly improbable. Understanding the consumer exposure Keywords: to enzymes which are used in laundry and cleaning products is a key step to the risk management pro- Enzymes Allergy cess. Validation of the risk assessment conclusions and the risk management process only comes with Asthma practical experience and evidence from the marketplace. In the present work, clinical data from a range IgE antibody of sources collected over the past 40 years have been analysed.
    [Show full text]
  • Combo Detergent Enzymes Types
    JIAAN Enzymes replacing Chemicals BIOTECH Biological washing pow- ders contain enzymes to help to re- move stains from clothes. They con- tain these enzymes: amylases DETERGENT (carbohydrases) - to digest starch. ENZYMES proteases - to digest protein and re- move protein stains (such as egg and blood) Most biological laundry deter- Combo Detergent gents contain lipase and protease enzymes, both of which are found in Enzymes Types: the body. Lipases break down fats and oils, while proteaseswork to JiaanD-Cocktail 1 break down protein chains. Their ability to break down the- JiaanD-Cocktail 2 se compoundsmakes them excel- JiaanD-Cocktail 3 lent for stain removal. J B HO - K T N P I MP F P N - S- A P MP E ID P - JIAAN ENZYMES - - Detergent Enzymes : Combo Packs These Enzymes are combination of various Enzymes , which are alternate to the traditional laundry detergents. Hence, these enzymes delivers powerful stain removal with the brilliance and fabric care benefits highly effective at the lower was temperature . Perfect Stain cleaning than the traditional chemical ingredients. 1. JiaanD-Cocktail 2 ADVANTAGES : Jiaan-D-Cocktail 2 is a combo of Protease, Lipase , Cellulase and Alpha amylase enzymes. Alternative to traditional laundry detergent, Jiaan-D- 1. Powerful stain cleaner than the traditional chemical Ingredients, removes Cocktail 2 delivers the powerful stain removal with the brilliance and fabric dirt & grease care benefits highly effective at the all wash temperature. Perfect stain clean- 2. Suitable with natural surfactants 3. Bio-based and readily bio-degradable ing than the traditional chemical ingredients. 4. Reduces the environmental load 5.
    [Show full text]
  • Novel Perspectives for Evolving Enzyme Cocktails for Lignocellulose
    Mohanram et al. Sustainable Chemical Processes 2013, 1:15 http://www.sustainablechemicalprocesses.com/content/1/1/15 REVIEW Open Access Novel perspectives for evolving enzyme cocktails for lignocellulose hydrolysis in biorefineries Saritha Mohanram, Dolamani Amat, Jairam Choudhary, Anju Arora* and Lata Nain Abstract The unstable and uncertain availability of petroleum sources as well as rising cost of fuels have shifted global efforts to utilize renewable resources for the production of greener energy and a replacement which can also meet the high energy demand of the world. Bioenergy routes suggest that atmospheric carbon can be cycled through biofuels in carefully designed systems for sustainability. Significant potential exists for bioconversion of biomass, the most abundant and also the most renewable biomaterial on our planet. However, the requirements of enzyme complexes which act synergistically to unlock and saccharify polysaccharides from the lignocellulose complex to fermentable sugars incur major costs in the overall process and present a great challenge. Currently available cellulase preparations are subject to tight induction and regulation systems and also suffer inhibition from various end products. Therefore, more potent and efficient enzyme preparations need to be developed for the enzymatic saccharification process to be more economical. Approaches like enzyme engineering, reconstitution of enzyme mixtures and bioprospecting for superior enzymes are gaining importance. The current scenario, however, also warrants the need for research and development of integrated biomass production and conversion systems. Keywords: Lignocellulose, Bioethanol, Cellulase, Hemicellulase, Bioprospecting, Enzymatic saccharification Introduction Investment into biofuels production capacity exceeded Increased public and scientific attention towards alterna- $4 billion worldwide in 2007 and is growing.
    [Show full text]
  • The Role of Enzymes in Modern Detergency
    REVIEW The Role of Enzymes in Modern Detergency Hans Sejr Olsen* and Per Falholt Enzyme Development & Application, Enzyme Business, Novo Nordisk A/S, DK-2880 Bagsvaerd, Denmark ABSTRACT: Enzymes have effectively assisted the develop- lulases, the foundations were already laid in 1913 for the ment and improvement of modern household and industrial de- commercial use of enzymes that continues to be important tergents. The major classes of detergent enzymes—proteases, li- today. pases, amylases, and cellulases—each provide specific benefits Today the most widely used industrial enzymes are hy- for application in laundry and automatic dishwashing. Histori- drolases, which remove soils based on proteins, lipids, and cally, proteases were first to be used extensively in laundry de- polysaccharides. Cellulolytic enzymes are another class of tergents. In addition to raising the level of cleaning, they have hydrolases that provide fabric care through selective reac- also provided environmental benefits by reducing energy con- sumption through shorter washing times, lower washing tem- tions not previously possible on fabrics. Research is cur- peratures, and reduced water consumption. Today proteases are rently underway into the possibility of using redox en- joined by lipases and amylases in improving detergent efficacy zymes—oxidases or peroxidases—for bleaching colored especially for household laundering at lower temperatures and, components (2). in industrial cleaning operations, at lower pH levels. Cellulases To support the 18–19-million -ton global annual market contribute to overall fabric care by rejuvenating or maintaining for laundry and dishwashing detergents (3), the world- the new appearance of washed garments. Enzymes are pro- wide consumption of detergent enzymes amounted to duced by fermentation technologies that utilize renewable re- ca.
    [Show full text]
  • Istanbul Technical University Institute of Science And
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE ISTANBUL TECHNICAL UNIVERSITY INSTITUTE OF SCIENCE AND TECHNOLOGY PARTIAL PURIFICATION AND CHARACTERIZATION OF ALKALINE PROTEASES FROM ISOLATED BACILLUS STRAINS M.Sc. Thesis by M.Hale Öztürk Department: Advanced Technologies Programme: Molecular Biology - Genetics & Biotechnology JANUARY 2005 ISTANBUL TECHNICAL UNIVERSITY INSTITUTE OF SCIENCE AND TECHNOLOGY PARTIAL PURIFICATION AND CHARACTERIZATION OF ALKALINE PROTEASES FROM ISOLATED BACILLUS STRAINS M.Sc. Thesis by M.Hale Öztürk (707021002) Date of submission : 27 December 2004 Date of defence examination : 25 January 2005 Supervisors : Assist. Prof. Dr. Hakan BERMEK Assoc. Prof. Dr. Yüksel AVCIBAŞI GÜVENİLİR Members of the Examining Committee : Prof. Dr. Bülent GÜRLER (İ.Ü.) Assist. Prof. Dr. Ayten YAZGAN KARATAŞ (İ.T.Ü.) Assist. Prof. Dr. Nevin GÜL KARAGÜLER (İ.T.Ü.) JANUARY 2005 İSTANBUL TEKNİK ÜNİVERSİTESİ FEN BİLİMLERİ ENSTİTÜSÜ İZOLE EDİLEN BACILLUS TÜRLERİNDEN ALKALİN PROTEAZ ENZİMİNİN KISMİ SAFLAŞTIRILMASI VE KARAKTERİZASYONU YÜKSEK LİSANS TEZİ Kim.Müh. M.Hale Öztürk (707021002) Tezin Enstitüye Verildiği Tarih : 27 Aralık 2004 Tezin Savunulduğu Tarih : 25 Ocak 2005 Tez Danışmanları : Yrd. Doç. Dr. Hakan BERMEK Doç. Dr. Yüksel AVCIBAŞI GÜVENİLİR Diğer Jüri Üyeleri : Prof. Dr. Bülent GÜRLER (İ.Ü.) Yrd. Doç. Dr. Ayten YAZGAN KARATAŞ (İ.T.Ü.) Yrd. Doç. Dr. Nevin GÜL KARAGÜLER (İ.T.Ü.) OCAK 2005 ACKNOWLEDGEMENTS I would like to thank to Assoc. Prof. Yüksel Avcıbaşı Güvenilir for being not only my supervisor but also for supporting, encouraging me in every step of this work. I would like to thank to my supervisor Assist. Prof. Hakan Bermek for his assistance during my thesis.
    [Show full text]
  • Stabilization of a Lipolytic Enzyme for Commercial Application
    Article Stabilization of a Lipolytic Enzyme for Commercial Application Simone Antonio De Rose 1, Halina Novak 1,†, Andrew Dowd 2,†, Sukriti Singh 2, Dietmar Andreas Lang 2 and Jennifer Littlechild 1,* 1 Henry Wellcome Building for Biocatalysis, Biosciences, College of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, UK; [email protected] (S.A.D.R.); [email protected] (H.N.) 2 Unilever R&D, HomeCare Discover, Disruptive Biotechnology, Quarry Road East, Bebington CH63 3JW, UK; [email protected] (A.D.); [email protected] (S.S.); [email protected] (D.A.L.) * Correspondence: [email protected]; Tel.: +44-0-1392-723468 † At the time of project execution. Academic Editor: David D. Boehr Received: 26 January 2017; Accepted: 10 March 2017; Published: 21 March 2017 Abstract: Thermomyces lanouginosa lipase has been used to develop improved methods for carrier- free immobilization, the Cross-Linked Enzyme Aggregates (CLEAs), for its application in detergent products. An activator step has been introduced to the CLEAs preparation process with the addition of Tween 80 as activator molecule, in order to obtain a higher number of the individual lipase molecules in the ”open lid” conformation prior to the cross-linking step. A terminator step has been introduced to quench the cross-linking reaction at an optimal time by treatment with an amine buffer in order to obtain smaller and more homogenous cross-linked particles. This improved immobilization method has been compared to a commercially available enzyme and has been shown to be made up of smaller and more homogenous particles with an average diameter of 1.85 ± 0.28 μm which are 129.7% more active than the free enzyme.
    [Show full text]
  • Go Molecular! a Clinical Reference Guide to Molecular Allergy Part 2: the Allergen Components
    Setting the standard in allergy diagnostics 2019 edition with the latest news in molecular allergology Go molecular! A clinical reference guide to molecular allergy Part 2: The allergen components Second edition | By Neal Bradshaw For more information on this topic allergyai.com Go molecular! Preface In the previous 2013 edition of Go the content in this new version of Go Molecular, I produced a straight forward Molecular has been aimed to provide clinical reference guide book to describe improved diagnostic explanations in common allergens and their constituent the form of tables, with concise clinical components. This guide is an update interpretation comments. Also new is a to the original but keeps the focus on section on aero-allergen components, understanding component test results, an introduction to micro-array, as well as well as what tests are actually as new information on diagnostic gaps commercial available (since this is an regarding certain food components. important practical aspect of molecular allergy!). If you need further supporting information relating to molecular allergy then I can Since 2013 the science of molecular recommend visiting our webpage: allergy has exploded with many new allergyai.com. studies both using single and multiplex allergen testing formats. There is a lot Neal Bradshaw of new clinical evidence to consider, Portfolio Manager - Allergy emerging allergens like alpha-gal and the Thermo Fisher Scientific availability of new ImmunoCAPTM Allergen Components. Beyond the new science, Disclaimer: The content of this book is intended as an aid to the physician to interpret allergen specific IgE antibody test results. It is not intended as medical advice on an individual level.
    [Show full text]
  • WO 2014/100018 Al 26 June 2014 (26.06.2014) W P O P C T
    (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2014/100018 Al 26 June 2014 (26.06.2014) W P O P C T (51) International Patent Classification: (81) Designated States (unless otherwise indicated, for every C12N 9/24 (2006.01) kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, (21) International Application Number: BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, PCT/US2013/075829 DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, (22) International Filing Date: HN, HR, HU, ID, IL, IN, IR, IS, JP, KE, KG, KN, KP, KR, 17 December 2013 (17. 12.2013) KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, (25) Filing Language: English OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, (26) Publication Language: English SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, (30) Priority Data: ZW. 61/739,267 19 December 2012 (19. 12.2012) US (84) Designated States (unless otherwise indicated, for every (71) Applicant: DANISCO US INC. [US/US]; 925 Page Mill kind of regional protection available): ARIPO (BW, GH, Road, Palo Alto, California 94304 (US). GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, SZ, TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, (72) Inventors: BARNETT, Christopher C ; Danisco US Inc., TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, DK, 925 Page Mill Road, Palo Alto, California 94304 (US).
    [Show full text]