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Microbial Enzymes and Their Applications in Industries and Medicine
BioMed Research International Microbial Enzymes and Their Applications in Industries and Medicine Guest Editors: Periasamy Anbu, Subash C. B. Gopinath, Arzu Coleri Cihan, and Bidur Prasad Chaulagain Microbial Enzymes and Their Applications in Industries and Medicine BioMed Research International Microbial Enzymes and Their Applications in Industries and Medicine Guest Editors: Periasamy Anbu, Subash C. B. Gopinath, Arzu Coleri Cihan, and Bidur Prasad Chaulagain Copyright © 2013 Hindawi Publishing Corporation. All rights reserved. This is a special issue published in “BioMed Research International.” All articles are open access articles distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Contents Microbial Enzymes and Their Applications in Industries and Medicine,PeriasamyAnbu, Subash C. B. Gopinath, Arzu Coleri Cihan, and Bidur Prasad Chaulagain Volume 2013, Article ID 204014, 2 pages Effect of C/N Ratio and Media Optimization through Response Surface Methodology on Simultaneous Productions of Intra- and Extracellular Inulinase and Invertase from Aspergillus niger ATCC 20611, Mojdeh Dinarvand, Malahat Rezaee, Malihe Masomian, Seyed Davoud Jazayeri, Mohsen Zareian, Sahar Abbasi, and Arbakariya B. Ariff Volume 2013, Article ID 508968, 13 pages A Broader View: Microbial Enzymes and Their Relevance in Industries, Medicine, and Beyond, Neelam Gurung, Sumanta Ray, Sutapa Bose, and Vivek Rai Volume 2013, Article -
Bacteria Belonging to Pseudomonas Typographi Sp. Nov. from the Bark Beetle Ips Typographus Have Genomic Potential to Aid in the Host Ecology
insects Article Bacteria Belonging to Pseudomonas typographi sp. nov. from the Bark Beetle Ips typographus Have Genomic Potential to Aid in the Host Ecology Ezequiel Peral-Aranega 1,2 , Zaki Saati-Santamaría 1,2 , Miroslav Kolaˇrik 3,4, Raúl Rivas 1,2,5 and Paula García-Fraile 1,2,4,5,* 1 Microbiology and Genetics Department, University of Salamanca, 37007 Salamanca, Spain; [email protected] (E.P.-A.); [email protected] (Z.S.-S.); [email protected] (R.R.) 2 Spanish-Portuguese Institute for Agricultural Research (CIALE), 37185 Salamanca, Spain 3 Department of Botany, Faculty of Science, Charles University, Benátská 2, 128 01 Prague, Czech Republic; [email protected] 4 Laboratory of Fungal Genetics and Metabolism, Institute of Microbiology of the Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic 5 Associated Research Unit of Plant-Microorganism Interaction, University of Salamanca-IRNASA-CSIC, 37008 Salamanca, Spain * Correspondence: [email protected] Received: 4 July 2020; Accepted: 1 September 2020; Published: 3 September 2020 Simple Summary: European Bark Beetle (Ips typographus) is a pest that affects dead and weakened spruce trees. Under certain environmental conditions, it has massive outbreaks, resulting in attacks of healthy trees, becoming a forest pest. It has been proposed that the bark beetle’s microbiome plays a key role in the insect’s ecology, providing nutrients, inhibiting pathogens, and degrading tree defense compounds, among other probable traits. During a study of bacterial associates from I. typographus, we isolated three strains identified as Pseudomonas from different beetle life stages. In this work, we aimed to reveal the taxonomic status of these bacterial strains and to sequence and annotate their genomes to mine possible traits related to a role within the bark beetle holobiont. -
Epidemiology of Mucopolysaccharidoses Update
diagnostics Review Epidemiology of Mucopolysaccharidoses Update Betul Celik 1,2 , Saori C. Tomatsu 2 , Shunji Tomatsu 1 and Shaukat A. Khan 1,* 1 Nemours/Alfred I. duPont Hospital for Children, Wilmington, DE 19803, USA; [email protected] (B.C.); [email protected] (S.T.) 2 Department of Biological Sciences, University of Delaware, Newark, DE 19716, USA; [email protected] * Correspondence: [email protected]; Tel.: +302-298-7335; Fax: +302-651-6888 Abstract: Mucopolysaccharidoses (MPS) are a group of lysosomal storage disorders caused by a lysosomal enzyme deficiency or malfunction, which leads to the accumulation of glycosaminoglycans in tissues and organs. If not treated at an early stage, patients have various health problems, affecting their quality of life and life-span. Two therapeutic options for MPS are widely used in practice: enzyme replacement therapy and hematopoietic stem cell transplantation. However, early diagnosis of MPS is crucial, as treatment may be too late to reverse or ameliorate the disease progress. It has been noted that the prevalence of MPS and each subtype varies based on geographic regions and/or ethnic background. Each type of MPS is caused by a wide range of the mutational spectrum, mainly missense mutations. Some mutations were derived from the common founder effect. In the previous study, Khan et al. 2018 have reported the epidemiology of MPS from 22 countries and 16 regions. In this study, we aimed to update the prevalence of MPS across the world. We have collected and investigated 189 publications related to the prevalence of MPS via PubMed as of December 2020. In total, data from 33 countries and 23 regions were compiled and analyzed. -
Hexosaminidase in Mast Β Primary Role of Degranulation Indicator in Mast Cells?
Does β-Hexosaminidase Function Only as a Degranulation Indicator in Mast Cells? The Primary Role of β-Hexosaminidase in Mast Cell Granules This information is current as of September 25, 2021. Nobuyuki Fukuishi, Shinya Murakami, Akane Ohno, Naoya Yamanaka, Nobuaki Matsui, Kenji Fukutsuji, Sakuo Yamada, Kouji Itoh and Masaaki Akagi J Immunol 2014; 193:1886-1894; Prepublished online 11 July 2014; Downloaded from doi: 10.4049/jimmunol.1302520 http://www.jimmunol.org/content/193/4/1886 http://www.jimmunol.org/ Supplementary http://www.jimmunol.org/content/suppl/2014/07/11/jimmunol.130252 Material 0.DCSupplemental References This article cites 52 articles, 18 of which you can access for free at: http://www.jimmunol.org/content/193/4/1886.full#ref-list-1 Why The JI? Submit online. by guest on September 25, 2021 • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2014 by The American Association of -
Product Guide
www.megazyme.com es at dr hy o rb a C • s e t a r t s b u S e m y z n E • s e m y z n E • s t i K y a s s A Plant Cell Wall & Biofuels Product Guide 1 Megazyme Test Kits and Reagents Purity. Quality. Innovation. Barry V. McCleary, PhD, DScAgr Innovative test methods with exceptional technical support and customer service. The Megazyme Promise. Megazyme was founded in 1988 with the We demonstrate this through the services specific aim of developing and supplying we offer, above and beyond the products we innovative test kits and reagents for supply. We offer worldwide express delivery the cereals, food, feed and fermentation on all our shipments. In general, technical industries. There is a clear need for good, queries are answered within 48 hours. To validated methods for the measurement of make information immediately available to the polysaccharides and enzymes that affect our customers, we established a website in the quality of plant products from the farm 1994, and this is continually updated. Today, it gate to the final food. acts as the source of a wealth of information on Megazyme products, but also is the hub The commitment of Megazyme to “Setting of our commercial activities. It offers the New Standards in Test Technology” has been possibility to purchase and pay on-line, to continually recognised over the years, with view order history, to track shipments, and Megazyme and myself receiving a number many other features to support customer of business and scientific awards. -
Quality Assessment Enzyme Analysis for Lysosomal Storage Diseases ERNDIM / EUGT Meeting 5-6 October 2006, Prague
QQuality Assessment Enzyme Analysis for Lysosomal Storage Diseases ERNDIM / EUGT meeting 5-6 October 2006, Prague Results of 1st “large scale” pilot Quality Assessment Enzyme Analysis for Lysosomal Storage Diseases Laboratories Rotterdam Hamburg/Heidelberg Dr, Zoltan Lukacs/Dr. Friederike Bürger QA-pilot for LSD’s the aims • Inter-laboratory variation ─ Many participants: > 30 • Intra-laboratory variation ─ Analyse two pairs of identical control samples (blind) • Proficiency testing of enzyme deficiencies ─ Which samples are best? - Blood samples: most widely used, but impractible - Fibroblasts: good but laborious - EBV lymphoblasts: easy to obtain, not widely used QA-pilot for LSD’s the set up • Samples, without clinical information ─ Leukocytes ─ EBV lymphoblasts ─ Fibroblasts • Enzymes: easy ones ─ 4MU-substrates ─ Simple colorimetric assays • Shipping: economic ─ Send at room temp., postal service - Lyophilised enzymes, stable at room temp. for 5 days - Fibroblasts • Data entry through existing ERNDIM programmes ─ “Metabolite presentation” (www.erndimqa.nl Æ Lysosomal Enzymes) QA-pilot for LSD’s the participants • Questionnaire to members (85 from 21 countries) ─ 40 labs want to join a QA-pilot ─ 65% want to include DBS in future QA-schemes • Samples sent, data returned ─ 40 labs received samples ─ 36 labs entered data on www.erndimqa.nl QA-pilot for LSD’s the samples • 10 samples ─ 4 leukocytes (two duplicate samples) ─ 4 EBV lymphoblasts ─ 2 fibroblasts • 10 easy enzymes ─ specific enzyme activity (e.g.. nmol/h/mg) ─ normalise to -
Cyclomaltodextrinase 13A, Paenibacillus Sp. Pcda13a (CBM34-GH13)
Cyclomaltodextrinase 13A, Paenibacillus sp. PCda13A (CBM34-GH13) Catalogue number: CZ08721 , 0,25 mg CZ08722 , 3 × 0,25 mg Description Storage temperature PCda13A (CBM34-GH13), E.C. number 3.2.1.54, is a This enzyme should be stored at -20 °C. cyclomaltodextrinase from Paenibacillus sp. Recombinant PCda13A (CBM34-GH13), purified from Escherichia coli , is a modular family 13 Glycoside Hydrolase (GH13) with an N-terminal Substrate specificity family 34 Carbohydrate Binding Module (CBM34) (www.cazy.org). The enzyme is provided in 35 mM NaHepes buffer, pH 7.5, 750 PCda13A (CBM34-GH13) hydrolyses α-, β-, and γ-cyclodextrins (CDs). The enzyme hydrolyze CDs and linear maltooligosaccharides mM NaCl, 200 mM imidazol, 3.5 mM CaCl 2 and 25% (v/v) glycerol, at a 0,25 mg/mL concentration. Bulk quantities of this product are to yield maltose and glucose with less amounts of maltotriose and available on request. maltotetraose. Electrophoretic Purity Temperature and pH optima PCda13A (CBM34-GH13) purity was determined by sodium The pH optimum for enzymatic activity is 7 while temperature dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) optimum is 40 °C. followed by BlueSafe staining (MB15201) (Figure 1). Enzyme activity Substrate specificity and kinetic properties of PCda13A (CBM34- GH13) are described in the reference provided below. Follow the instructions described in the paper for the implementation of enzyme assays and to obtain values of specific activity. To measure catalytic activity of GHs, quantify reducing sugars released from polysaccharides through the method described by Miller (1959; Anal. Chem. 31, 426-428). Reference Kaulpiboon and Pongsawasdi. J Biochem Mol Biol. -
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. -
DRUGS REQUIRING PRIOR AUTHORIZATION in the MEDICAL BENEFIT Page 1
Effective Date: 08/01/2021 DRUGS REQUIRING PRIOR AUTHORIZATION IN THE MEDICAL BENEFIT Page 1 Therapeutic Category Drug Class Trade Name Generic Name HCPCS Procedure Code HCPCS Procedure Code Description Anti-infectives Antiretrovirals, HIV CABENUVA cabotegravir-rilpivirine C9077 Injection, cabotegravir and rilpivirine, 2mg/3mg Antithrombotic Agents von Willebrand Factor-Directed Antibody CABLIVI caplacizumab-yhdp C9047 Injection, caplacizumab-yhdp, 1 mg Cardiology Antilipemic EVKEEZA evinacumab-dgnb C9079 Injection, evinacumab-dgnb, 5 mg Cardiology Hemostatic Agent BERINERT c1 esterase J0597 Injection, C1 esterase inhibitor (human), Berinert, 10 units Cardiology Hemostatic Agent CINRYZE c1 esterase J0598 Injection, C1 esterase inhibitor (human), Cinryze, 10 units Cardiology Hemostatic Agent FIRAZYR icatibant J1744 Injection, icatibant, 1 mg Cardiology Hemostatic Agent HAEGARDA c1 esterase J0599 Injection, C1 esterase inhibitor (human), (Haegarda), 10 units Cardiology Hemostatic Agent ICATIBANT (generic) icatibant J1744 Injection, icatibant, 1 mg Cardiology Hemostatic Agent KALBITOR ecallantide J1290 Injection, ecallantide, 1 mg Cardiology Hemostatic Agent RUCONEST c1 esterase J0596 Injection, C1 esterase inhibitor (recombinant), Ruconest, 10 units Injection, lanadelumab-flyo, 1 mg (code may be used for Medicare when drug administered under Cardiology Hemostatic Agent TAKHZYRO lanadelumab-flyo J0593 direct supervision of a physician, not for use when drug is self-administered) Cardiology Pulmonary Arterial Hypertension EPOPROSTENOL (generic) -
Expression of Cyclomaltodextrinase Gene from Bacillus Halodurans C-125 and Characterization of Its Multisubstrate Specificity
Food Sci. Biotechnol. Vol. 18, No. 3, pp. 776 ~ 781 (2009) ⓒ The Korean Society of Food Science and Technology Expression of Cyclomaltodextrinase Gene from Bacillus halodurans C-125 and Characterization of Its Multisubstrate Specificity Hye-Jeong Kang, Chang-Ku Jeong, Myoung-Uoon Jang, Seung-Ho Choi, Min-Hong Kim1, Jun-Bae Ahn2, Sang-Hwa Lee3, Sook-Ja Jo3, and Tae-Jip Kim* Department of Food Science and Technology, Chungbuk National University, Cheongju, Chungbuk 361-763, Korea 1MH2 Biochemical Co., Ltd., Eumseong, Chungbuk 369-841, Korea 2Department of Food Service Industry, Seowon University, Cheongju, Chungbuk 361-741, Korea 3Department of Food and Nutrition, Seowon University, Cheongju, Chungbuk 361-741, Korea Abstract A putative cyclomaltodextrinase (BHCD) gene was found from the genome of Bacillus halodurans C-125, which encodes 578 amino acids with a predicted molecular mass of 67,279 Da. It shares 42-59% of amino acid sequence identity with common cyclomaltodextrinase (CDase)-family enzymes. The corresponding gene was cloned by polymerase chain reaction (PCR) and the dimeric enzyme with C-terminal 6-histidines was successfully overproduced and purified from recombinant Escherichia coli. BHCD showed the highest activity against β-CD at pH 7.0 and 50oC. Due to its versatile hydrolysis and transglycosylation activities, BHCD has been confirmed as a member of CDases. However, BHCD can be distinguished from other typical CDases on the basis of its novel multisubstrate specificity. While typical CDases have over 10 times higher activity on β-CD than starch or pullulan, the CD-hydrolyzing activity of BHCD is only 2.3 times higher than pullulan. -
Functional Characterization of Carbohydrate-Active Enzymes from Marine Bacteria
Functional characterization of carbohydrate-active enzymes from marine bacteria I n a u g u r a l d i s s e r t a t i o n zur Erlangung des akademischen Grades eines Doktors der Naturwissenschaften (Dr. rer. nat.) der Mathematisch-Naturwissenschaftlichen Fakultät der Universität Greifswald vorgelegt von Marcus Bäumgen Greifswald, 28.02.2020 Dekan: Prof. Dr. Werner Weitschies 1. Gutachter: Prof. Dr. Uwe T. Bornscheuer 2. Gutachter: Prof. Dr. Harry Brumer Tag der Promotion: 24.06.2020 II III Wissenschaft ist das Werkzeug, welches es uns ermöglicht, das große Puzzel der Natur und des Lebens zu lösen. IV Auch wenn wir den Weg des Wissens und der Weisheit niemals bis zum Ende beschreiten können, so ist doch jeder Schritt, den wir tun, ein Schritt in eine bessere Welt. V Content Abbreviations ..................................................................................................................... IX 1. Introduction ..................................................................................................................... 1 1.1 The marine carbon cycle .............................................................................................. 1 1.1.1 Algal blooms .......................................................................................................... 1 1.1.2 The marine carbohydrates ulvan and xylan ........................................................... 2 1.1.3 Marine polysaccharide utilization ........................................................................... 4 1.2 Carbohydrate-active enzymes -
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.