Comparative Genomics and Physiological Investigation Supported Safety, Cold Adaptation, Efficient Hydrolytic and Plant Growth Promoting Potential of Psychrotrophic
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Advances in Chitin/Chitosan Characterization and Applications
Advances in Chitin/Chitosan Characterization and Applications Edited by Marguerite Rinaudo and Francisco M. Goycoolea Printed Edition of the Special Issue Published in Polymers www.mdpi.com/journal/polymers Advances in Chitin/Chitosan Characterization and Applications Advances in Chitin/Chitosan Characterization and Applications Special Issue Editors Marguerite Rinaudo Francisco M. Goycoolea MDPI • Basel • Beijing • Wuhan • Barcelona • Belgrade Special Issue Editors Marguerite Rinaudo Francisco M. Goycoolea University of Grenoble Alpes University of Leeds France UK Editorial Office MDPI St. Alban-Anlage 66 4052 Basel, Switzerland This is a reprint of articles from the Special Issue published online in the open access journal Polymers (ISSN 2073-4360) from 2017 to 2018 (available at: https://www.mdpi.com/journal/polymers/ special issues/chitin chitosan) For citation purposes, cite each article independently as indicated on the article page online and as indicated below: LastName, A.A.; LastName, B.B.; LastName, C.C. Article Title. Journal Name Year, Article Number, Page Range. ISBN 978-3-03897-802-2 (Pbk) ISBN 978-3-03897-803-9 (PDF) c 2019 by the authors. Articles in this book are Open Access and distributed under the Creative Commons Attribution (CC BY) license, which allows users to download, copy and build upon published articles, as long as the author and publisher are properly credited, which ensures maximum dissemination and a wider impact of our publications. The book as a whole is distributed by MDPI under the terms and conditions of the Creative Commons license CC BY-NC-ND. Contents About the Special Issue Editors ..................................... ix Preface to ”Advances in Chitin/Chitosan Characterization and Applications” ......... -
Reduction of Pectinesterase Activity in a Commercial Enzyme Preparation
Journal of the Science of Food and Agriculture J Sci Food Agric 85:1613–1621 (2005) DOI: 10.1002/jsfa.2154 Reduction of pectinesterase activity in a commercial enzyme preparation by pulsed electric fields: comparison of inactivation kinetic models Joaquın´ Giner, Pascal Grouberman, Vicente Gimeno and Olga Martın´ ∗ Department of Food Technology, University of Lleida, CeRTA-UTPV, ETSEA, Avda Alcalde Rovira Roure 191, 25198-Lleida, Spain Abstract: The inactivation of pectinesterase (PE) in a commercial enzyme preparation (CEP) under high intensity pulsed electric fields (HIPEF) was studied. After desalting and water dilution of the raw CEP, samples were exposed to exponentially decay waveform pulses for up to 463 µs at electric field intensities ranging from 19 to 38 kV cm−1. Pulses were applied in monopolar mode. Experimental data were fitted to a first-order kinetic model as well as to models based on Fermi, Hulsheger¨ or Weibull equations to describe PE inactivation kinetics. Characteristic parameters for each model were calculated. Relationships between some of the parameters and process variables were obtained. The Weibull model yielded the best accuracy factor. The relationship between residual PE and input of electrical energy density was found to be that of exponential decay. 2005 Society of Chemical Industry Keywords: pulsed electric fields; kinetics; pectinesterase; model; inactivation INTRODUCTION It has become customary to use CEPs in fruit and Pectinesterase (PE; EC 3.1.1.11) is a pectic enzyme vegetable juice technology. Depending -
Yeast Genome Gazetteer P35-65
gazetteer Metabolism 35 tRNA modification mitochondrial transport amino-acid metabolism other tRNA-transcription activities vesicular transport (Golgi network, etc.) nitrogen and sulphur metabolism mRNA synthesis peroxisomal transport nucleotide metabolism mRNA processing (splicing) vacuolar transport phosphate metabolism mRNA processing (5’-end, 3’-end processing extracellular transport carbohydrate metabolism and mRNA degradation) cellular import lipid, fatty-acid and sterol metabolism other mRNA-transcription activities other intracellular-transport activities biosynthesis of vitamins, cofactors and RNA transport prosthetic groups other transcription activities Cellular organization and biogenesis 54 ionic homeostasis organization and biogenesis of cell wall and Protein synthesis 48 plasma membrane Energy 40 ribosomal proteins organization and biogenesis of glycolysis translation (initiation,elongation and cytoskeleton gluconeogenesis termination) organization and biogenesis of endoplasmic pentose-phosphate pathway translational control reticulum and Golgi tricarboxylic-acid pathway tRNA synthetases organization and biogenesis of chromosome respiration other protein-synthesis activities structure fermentation mitochondrial organization and biogenesis metabolism of energy reserves (glycogen Protein destination 49 peroxisomal organization and biogenesis and trehalose) protein folding and stabilization endosomal organization and biogenesis other energy-generation activities protein targeting, sorting and translocation vacuolar and lysosomal -
Review Article Pullulanase: Role in Starch Hydrolysis and Potential Industrial Applications
Hindawi Publishing Corporation Enzyme Research Volume 2012, Article ID 921362, 14 pages doi:10.1155/2012/921362 Review Article Pullulanase: Role in Starch Hydrolysis and Potential Industrial Applications Siew Ling Hii,1 Joo Shun Tan,2 Tau Chuan Ling,3 and Arbakariya Bin Ariff4 1 Department of Chemical Engineering, Faculty of Engineering and Science, Universiti Tunku Abdul Rahman, 53300 Kuala Lumpur, Malaysia 2 Institute of Bioscience, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia 3 Institute of Biological Sciences, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia 4 Department of Bioprocess Technology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia Correspondence should be addressed to Arbakariya Bin Ariff, [email protected] Received 26 March 2012; Revised 12 June 2012; Accepted 12 June 2012 Academic Editor: Joaquim Cabral Copyright © 2012 Siew Ling Hii et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The use of pullulanase (EC 3.2.1.41) has recently been the subject of increased applications in starch-based industries especially those aimed for glucose production. Pullulanase, an important debranching enzyme, has been widely utilised to hydrolyse the α-1,6 glucosidic linkages in starch, amylopectin, pullulan, and related oligosaccharides, which enables a complete and efficient conversion of the branched polysaccharides into small fermentable sugars during saccharification process. The industrial manufacturing of glucose involves two successive enzymatic steps: liquefaction, carried out after gelatinisation by the action of α- amylase; saccharification, which results in further transformation of maltodextrins into glucose. -
2010 Physical Biosciences Research Meeting
2010 Physical Biosciences Research Meeting Sheraton Inner Harbor Hotel Baltimore, MD October 17-20, 2010 Office of Basic Energy Sciences Chemical Sciences, Geosciences & Biosciences Division 2010 Physical Biosciences Research Meeting Program and Abstracts Sheraton Inner Harbor Hotel Baltimore, MD October 17-20, 2010 Chemical Sciences, Geosciences, and Biosciences Division Office of Basic Energy Sciences Office of Science U.S. Department of Energy i Cover art is taken from the public domain and can be found at: http://commons.wikimedia.org/wiki/File:Blue_crab_on_market_in_Piraeus_-_Callinectes_sapidus_Rathbun_20020819- 317.jpg This document was produced under contract number DE-AC05-060R23100 between the U.S. Department of Energy and Oak Ridge Associated Universities. The research grants and contracts described in this document are, unless specifically labeled otherwise, supported by the U.S. DOE Office of Science, Office of Basic Energy Sciences, Chemical Sciences, Geosciences, and Biosciences Division. ii Foreword This volume provides a record of the 2nd biennial meeting of the Principal Investigators (PIs) funded by the Physical Biosciences program, and is sponsored by the Chemical Sciences, Geosciences, and Biosciences Division of the Office of Basic Energy Sciences (BES) in the U.S. Department of Energy (DOE). Within DOE-BES there are two programs that fund basic research in energy-relevant biological sciences, Physical Biosciences and Photosynthetic Systems. These two Biosciences programs, along with a strong program in Solar Photochemistry, comprise the current Photo- and Bio- Chemistry Team. This meeting specifically brings together under one roof all of the PIs funded by the Physical Biosciences program, along with Program Managers and staff not only from DOE-BES, but also other offices within DOE, the national labs, and even other federal funding agencies. -
GRAS Notice 975, Maltogenic Alpha-Amylase Enzyme Preparation
GRAS Notice (GRN) No. 975 https://www.fda.gov/food/generally-recognized-safe-gras/gras-notice-inventory novozyme~ Rethink Tomorrow A Maltogenic Alpha-Amylase from Geobacillus stearothermophilus Produced by Bacillus licheniformis Janet Oesterling, Regulatory Affairs, Novozymes North America, Inc., USA October 2020 novozyme~ Reth in k Tomorrow PART 2 - IDENTITY, METHOD OF MANUFACTURE, SPECIFICATIONS AND PHYSICAL OR TECHNICAL EFFECT OF THE NOTIFIED SUBSTANCE ..................................................................... 4 2.1 IDENTITY OF THE NOTIFIED SUBSTANCE ................................................................................ 4 2.2 IDENTITY OF THE SOURCE ......................................................................................................... 4 2.2(a) Production Strain .................................................................................................. 4 2.2(b) Recipient Strain ..................................................................................................... 4 2.2(c) Maltogenic Alpha-Amylase Expression Plasmid ................................................... 5 2.2(d) Construction of the Recombinant Microorganism ................................................. 5 2.2(e) Stability of the Introduced Genetic Sequences .................................................... 5 2.2(f) Antibiotic Resistance Gene .................................................................................. 5 2.2(g) Absence of Production Organism in Product ...................................................... -
Download Product Insert (PDF)
PRODUCT INFORMATION Lysophospholipase D Polyclonal Antibody Item No. 10005375 Overview and Properties Contents: This vial contains 500 µl of peptide affinity-purified antibody. Synonyms: Autotaxin, ENPP2, lysoPLD Immunogen: Peptide from the C-terminal region of rat LysoPLD Species Reactivity: (+) Human, mouse, and rat; other species not tested Form: Liquid Storage: -20°C (as supplied) Stability: ≥1 year Storage Buffer: TBS, pH 7.4, with 50% glycerol, 0.1%l BSA, and 0.02% sodium azide Host: Rabbit Applications: Immunocytochemistry (ICC), Immunohistochemistry (IHC), and Western blot (WB); the recommended starting dilution for ICC is 1:500, 1:80 for IHC, and 1:200 for WB. Other applications were not tested, therefore optimal working concentration/dilution should be determined empirically. Images 1 · · · · · · · 104 kDa · · · · · · · 60 kDa Lane 1: Human cerebella supernatant (40 µg) Immunohistochemistry analysis of formalin-fixed, paraffin-embedded (FFPE) human cerebellum ǎssue aer heat-induced anǎgen retrieval in pH 6.0 citrate buffer. Aer incubaǎon with Lysophospholipase D Polyclonal Anǎbody (Item No. 10005375) at a 1:80 diluǎon, slides were incubated with bioǎnylated secondary anǎbody, followed by alkaline phosphatase-strepavidin and chromogen (DAB). WARNING CAYMAN CHEMICAL THIS PRODUCT IS FOR RESEARCH ONLY - NOT FOR HUMAN OR VETERINARY DIAGNOSTIC OR THERAPEUTIC USE. 1180 EAST ELLSWORTH RD SAFETY DATA ANN ARBOR, MI 48108 · USA This material should be considered hazardous until further information becomes available. Do not ingest, inhale, get in eyes, on skin, or on clothing. Wash thoroughly after handling. Before use, the user must review the complete Safety Data Sheet, which has been sent via email to your institution. PHONE: [800] 364-9897 WARRANTY AND LIMITATION OF REMEDY [734] 971-3335 Buyer agrees to purchase the material subject to Cayman’s Terms and Conditions. -
Generate Metabolic Map Poster
Authors: Pallavi Subhraveti Ron Caspi Peter Midford Peter D Karp 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. Ingrid Keseler Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Gcf_001591825Cyc: Bacillus vietnamensis NBRC 101237 Cellular Overview Connections between pathways are omitted for legibility. Anamika Kothari sn-glycerol phosphate phosphate pro phosphate phosphate phosphate thiamine molybdate D-xylose D-ribose glutathione 3-phosphate D-mannitol L-cystine L-djenkolate lanthionine α,β-trehalose phosphate phosphate [+ 3 more] α,α-trehalose predicted predicted ABC ABC FliY ThiT XylF RbsB RS10935 UgpC TreP PutP RS10200 PstB PstB RS10385 RS03335 RS20030 RS19075 transporter transporter of molybdate of phosphate α,β-trehalose 6-phosphate L-cystine D-xylose D-ribose sn-glycerol D-mannitol phosphate phosphate thiamine glutathione α α phosphate phosphate phosphate phosphate L-djenkolate 3-phosphate , -trehalose 6-phosphate pro 1-phosphate lanthionine molybdate phosphate [+ 3 more] Metabolic Regulator Amino Acid Degradation Amine and Polyamine Biosynthesis Macromolecule Modification tRNA-uridine 2-thiolation Degradation ATP biosynthesis a mature peptidoglycan a nascent β an N-terminal- -
Application A1204 Βeta-Amylase from Soybean (Glycine Max)
OFFICIAL 27 October 2020 [139-20] Supporting document 1 Risk and Technical assessment – Application A1204 Βeta-amylase from soybean (Glycine max) as a processing aid (enzyme) Executive summary The purpose of the application is to amend Schedule 18 – Processing Aids of the Australia New Zealand Food Standards Code (the Code) to include the enzyme beta-amylase (β- amylase) (EC 3.2.1.2) produced from soybeans (Glycine max). β-Amylase is proposed as a processing aid in starch processing for the production of maltose syrup. The evidence presented to support the proposed use of the enzyme provides adequate assurance that the enzyme, in the quantity and form proposed to be used, is technologically justified and has been demonstrated to be effective in achieving its stated purpose. The enzyme meets international identity and purity specifications. β-Amylase from soybean is derived from the edible parts of the Glycine max plant, for which a history of safe use over generations is well known. FSANZ considers that soybean β-amylase is unlikely to pose an allergenicity concern. Bioinformatic analysis identified a degree of amino acid sequence homology between β- amylase from soybean and an allergenic protein from wheat, but FSANZ does not consider β-amylase to be of allergenic concern in wheat allergic individuals given the likely very low exposure and that the enzyme is likely to be digested in the stomach like other dietary proteins. The WHO/IUIS Allergen Nomenclature Database lists seven soy proteins that are food allergens. β-amylase from soybean is not one of these seven allergenic soy proteins and is not an allergen to individuals with soybean food allergy. -
Generated by SRI International Pathway Tools Version 25.0, Authors S
Authors: Pallavi Subhraveti Ron Caspi Quang Ong Peter D Karp 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. Ingrid Keseler Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Gcf_000725805Cyc: Streptomyces xanthophaeus Cellular Overview Connections between pathways are omitted for legibility. -
Diagnostic Value of Serum Enzymes-A Review on Laboratory Investigations
Review Article ISSN 2250-0480 VOL 5/ ISSUE 4/OCT 2015 DIAGNOSTIC VALUE OF SERUM ENZYMES-A REVIEW ON LABORATORY INVESTIGATIONS. 1VIDYA SAGAR, M.SC., 2DR. VANDANA BERRY, MD AND DR.ROHIT J. CHAUDHARY, MD 1Vice Principal, Institute of Allied Health Sciences, Christian Medical College, Ludhiana 2Professor & Ex-Head of Microbiology Christian Medical College, Ludhiana 3Assistant Professor Department of Biochemistry Christian Medical College, Ludhiana ABSTRACT Enzymes are produced intracellularly, and released into the plasma and body fluids, where their activities can be measured by their abilities to accelerate the particular chemical reactions they catalyze. But different serum enzymes are raised when different tissues are damaged. So serum enzyme determination can be used both to detect cellular damage and to suggest its location in situ. Some of the biochemical markers such as alanine aminotransferase, aspartate aminotransferase, alkaline phasphatase, gamma glutamyl transferase, nucleotidase, ceruloplasmin, alpha fetoprotein, amylase, lipase, creatine phosphokinase and lactate dehydrogenase are mentioned to evaluate diseases of liver, pancreas, skeletal muscle, bone, etc. Such enzyme test may assist the physician in diagnosis and treatment. KEYWORDS: Liver Function tests, Serum Amylase, Lipase, CPK and LDH. INTRODUCTION mitochondrial AST is seen in extensive tissue necrosis during myocardial infarction and also in chronic Liver diseases like liver tissue degeneration DIAGNOSTIC SERUM ENZYME and necrosis². But lesser amounts are found in Enzymes are very helpful in the diagnosis of brain, pancreas and lung. Although GPT is plentiful cardiac, hepatic, pancreatic, muscular, skeltal and in the liver and occurs only in the small amount in malignant disorders. Serum for all enzyme tests the other tissues. -
What Is Alkaline Phosphatase? What Are the Symptoms of Low ALP?
What is the treatment for HPP? In 2015, asfotase alfa (Strensiq™) was approved for use in the US, the European Union, and Canada for pediatric-onset HPP, and in Japan for HPP with onset at any age. The medication is an injection given multiple times per week underneath the skin (subcutaneous). It is a recombinant (factory-made) form of ALP that has a bone-targeting component. When patients take asfotase alfa, ALP levels measured in the blood are quite high (often in the multiple thousands). Therefore, measuring ALP levels is typically not helpful once a patient is on therapy. What is Alkaline Phosphatase? What are the symptoms of low ALP? For more information, please contact Patients with hypophosphatasia (HPP) have Low ALP can lead to multiple symptoms of HPP, the Soft Bones Foundation. a low blood alkaline phosphatase (ALP) level. including poor bone mineralization and rickets as well (866) 827-9937 – Toll Free as early tooth loss (prior to age 5 years). It is also (973) 453-3093 – Direct Line thought that PPi may build up in muscle tissue 121 Hawkins Place, #267 ALP is an enzyme (a protein that breaks down and may be responsible for the pain and muscle Boonton, New Jersey 07005 chemicals). Most health providers are aware that weakness that some patients with HPP experience. www.SoftBones.org high ALP levels may indicate medical problems, such as liver disease or other bone diseases besides HPP, but many providers may not recognize that low ALP levels can indicate HPP. Low ALP is important What questions should patients ask Written by because the inability to break down chemicals can their doctors about ALP? Jill Simmons, MD lead to elevated levels of these chemicals, which Associate Professor of Pediatrics, Ian Burr Division can cause multiple problems.