DOCSLIB.ORG

Production and Molecular Characterization of Peroxidases

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text

Load more

PRODUCTION AND MOLECULAR CHARACTERIZATION OF PEROXIDASES FROM NOVEL LIGNINOLYTIC PROTEOBACTERIA AND BACILLUS STRAINS FALADE AYODEJI OSMUND 2018 PRODUCTION AND MOLECULAR CHARACTERIZATION OF PEROXIDASES FROM NOVEL LIGNINOLYTIC PROTEOBACTERIA AND BACILLUS STRAINS BY FALADE AYODEJI OSMUND (201508654) A THESIS SUBMITTED IN FULFILMENT OF THE REQUIREMENTS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY IN BIOCHEMISTRY DEPARTMENT OF BIOCHEMISTRY AND MICROBIOLOGY FACULTY OF SCIENCE AND AGRICULTURE UNIVERSITY OF FORT HARE ALICE, 5700 SOUTH AFRICA SUPERVISOR: PROF. L. V. MABINYA CO-SUPERVISOR: PROF. U. U. NWODO 2018 DECLARATION I, the undersigned, declare that this thesis entitled “Production and molecular characterization of peroxidases from novel ligninolytic proteobacteria and bacillus strains” submitted to the University of Fort Hare for the degree of Doctor of Philosophy in Biochemistry in the Faculty of Science and Agriculture is my original work and that the work has not been submitted to any other University in partial or entirely for the award of any degree or examination purposes. Name: Falade Ayodeji Osmund Signature: ………………………… Date: ………………………… ii DECLARATION ON PLAGIARISM I, Falade Ayodeji Osmund, student number: 201508654 hereby declare that I am fully aware of the University of Fort Hare’s policy on plagiarism and I have taken every precaution to comply with the regulations. Signature.………………………….. Date.………………………….. iii DECLARATION ON RESEARCH ETHICAL CLEARANCE I, Falade Ayodeji Osmund, student number: 201508654 hereby declare that I am fully aware of the University of Fort Hare’s policy on research ethics and I have taken every precaution to comply with the regulations. I confirm that my research constitutes an exemption to Rule G17.6.10.5 and an ethical certificate with a reference number is not required. Signature.………………………….. Date.………………………….. iv CERTIFICATION This thesis entitled “Production and molecular characterization of peroxidases from novel ligninolytic proteobacteria and bacillus strains” meets the regulation governing the award of degree of Doctor of Philosophy of the University of Fort Hare and is approved for its contribution to scientific knowledge. ……………………………………… …………………………… Prof. L. V. Mabinya Date Supervisor …………………………………… …………………………… Prof. U. U. Nwodo Date Co-supervisor and Head of Department v DEDICATION This thesis is dedicated to God Almighty, the giver of life; and in loving memory of my late Father, Mr. Johnson Akin Falade, who passed on in the course of this study. “…it is not of him that willeth, nor of him that runneth, but of God that sheweth mercy” Rom. 9:16 (KJV) vi ACKNOWLEDGMENTS Firstly, I humbly and sincerely thank the Almighty God for the gift of life and for blessing me with the required wisdom for this study as “…a man can receive nothing, except it be given him from heaven”. I wish to express my profound gratitude to Prof. A. I. Okoh for accepting me for a PhD study in his prestigious research group, Applied and Environmental Microbiology Research Group (AEMREG). No doubt, his kind gesture has in no small measure contributed to the realization of my academic dream. I would like to express my heartfelt appreciation to my supervisors, Prof. L. V. Mabinya and Prof. U. U. Nwodo for their constructive criticisms, inputs, corrections and insightful comments. Beyond their supervisory roles, they have been sources of inspiration to me throughtout the period of this study. Their wealth of experience has in no doubt contributed immensely to the success of this study. The technical supports and encouragements from my senior colleague, Dr. (Mrs) Evlyn Fatokun and the following colleagues: John Unuofin, Charles Osunla, Taiwo Fadare, Tayo Abioye, Kayode Afolabi, Tennison Digban, Rev. Sister Eyisi, Nonso Nnolim, Olusesan Adelabu, Tosin Olasehinde, Cyrus Ekundayo and Aboi Igwaran are gratefully acknowledged. The advice and supports of the following post doctoral fellows: Dr. Ben Iweriebor, Dr. Kunle Okayeito, Dr. Martins Adefisoye, Dr. Nolwazi Bhembe and Dr. Goke Adeniji are also acknowledged. More so, I wish to extend my sincere appreciation to all members of AEMREG and Biocatalysis/Biomolecules sub-group for their constructive criticisms and contributions toward the success of this study. Furthermore, I am very grateful to my mother, Mrs. Victoria Ajibola Falade and my parents-in- law, Chief and Mrs. Ayodele Omotayo for their prayers, encouragements and financial supports throughout the period of this study. May the good Lord bless you with long lives to enjoy the fruit of your labour in Jesus name (Amen). I would like to specially thank my sister, Mrs. Funmilayo Olaitan for her financial contribution towards the success of my PhD study, you have been a pillar of support; which has always proven to me that “blood is thicker than water”. May God reward your labour of love in Jesus name (Amen). Similarly, the moral and financial supports from my brother, Mr. Kole Falade and brothers-in-law, Messrs Ope, Seun, Lekan and Tubosun Omotayo vii are gratefully acknowledged. I would also like to thank my brother, Mr. Israel Orimoloye for his moral support during this study. This study would not have been a success without the prayers and support of my beautiful jewel, Mrs. Monisola Ayodeji-Falade, thank you for believing in my dreams and aspirations. I love you. This section would not be completed without appreciating my lovely kids: Praise and Caleb for their understanding and endurance throughout the period of this study. Daddy loves you. I thank Dr. J. O. Obameso for designing the primers used in this study. I also thank Dr. A. B. Falowo for proofreading part of this thesis and for his moral support. More so, I thank the management of the Federal University of Technology, Akure, Nigeria for granting me leave of absence to pursue my PhD programme. In conclusion, the financial supports from the National Research Foundation (NRF) under the South Africa/Tunisia bilateral collaboration (grant number: 95364), the South African Medical Research Council (SAMRC) and the Govan Mbeki Research and Development Centre (GMRDC) of the University of Fort Hare are gratefully acknowledged. viii LIST OF PUBLICATIONS FROM THIS THESIS Journal articles i. Falade, A. O., Nwodo, U. U., Iweriebor, B. C., Green, E., Mabinya, L. V. and Okoh, A. I. (2017). Lignin peroxidase functionalities and prospective applications. Microbiology Open 6, e00394. ii. Falade, A. O., Eyisi, O. A. L., Mabinya, L. V., Nwodo, U. U. and Okoh, A. I. (2017). Peroxidase production and ligninolytic potentials of freshwater bacteria Raoultella ornithinolytica and Ensifer adhaerens. Biotechnology Reports 16, 12-17. Conference proceedings i. Falade, A. O., Mabinya, L. V., Jaouani, A., Nwodo, U. U. and Okoh, A. I. (2016). Ligninolytic and peroxidase production potentials of novel bacterial strains isolated from freshwater and terrestrial milieux of the Nkonkobe Municipality, Eastern Cape, South Africa. Proceedings of the 1st Tunisian-South African International Conference, ISBST, Sidi Thabet, Tunisia (4 – 6 November, 2016). Oral. ii. Falade, A. O., Mabinya, L. V., Nwodo, U. U. and Okoh, A. I. (2018). Peroxidase production by Raoultella ornithinolytica OKOH-1 isolated from Tyhume river sediments. Proceedings of the Biennial Conference of the South African Society for Microbiology (SASM) held in Misty Hills Hotel and Conference Centre, Muldersdrift, Johannesburg, South Africa (4 – 7 April, 2018). Oral. ix LIST OF SUBMITTED MANUSCRIPTS i. Versatile peroxidase functionality: elimination of endocrine disrupting chemicals in wastewater. ii. Peroxidase produced by ligninolytic Bacillus species isolated from marsh and grassland decolourized anthraquinone and azo dyes. iii. Optimized peroxidase production and detection of catalase-peroxidase gene (KatG) in a Bacillus species isolated from Hogsback forest reserve, South Africa. iv. Optimization of process parameters for exoperoxidase production by Ensifer adhaerens NWODO-2 and PCR detection of catalase-peroxidase gene (KatG). v. Peroxidase production by a novel ligninolytic proteobacteria strain: Raoultella ornithinolytica OKOH-1. vi. Biochemical and molecular characterization of Raoultella ornithinolytica peroxidase with biotechnological potentials in dye decolourization and development of cosmetic agent. x LIST OF ACRONYMS 2, 4-DCP: 2, 4-Dichlorophenol ABTS: 2,2´-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) AC: Ammonium Chloride AEMREG: Applied and Environmental Microbiology Research Group AN: Ammonium Nitrate ANOVA: Analysis of Variance APEs: Alkylphenol Ethoxylates APs: Alkylphenols AS: Ammonium Sulphate AZB: Azure B B[a]P: Benzo [a] Pyrene BBD: Box-Behnken Design BGL: β-glucosidase BLAST: Basic Local Alignment Search Tools BPA: Bisphenol A BSA: Bovine Serum Albumin CCD: Central Composite Design CcP: Cytochrome c Peroxidase CLEA: Cross Linked Enzyme Aggregates CR: Congo Red DDT: Dichlorodiphenyltrichloroethane DiHCcP: Di-heme Cytochrome c Peroxidase DNA: Deoxyribonucleic Acid DOPA: Dihydroxyphenylalanine DyP: Dye decolourizing Peroxidase EDC: Endocrine Disrupting Chemicals EDTA: Ethylenediaminetetraacetic acid EMR: Enzymatic Membrane Reactor FPase: Filter Paper Cellulase GA: Guaiacol xi GMRDC: Govan Mbeki Research and Development Centre HPI: Hydroperoxidase I HRP: Horseradish Peroxidase KatG: Catalase-peroxidase KL: Kraft Lignin KTBA: α-keto-γ-thiomethylbutyric acid LiP: Lignin Peroxidase LMEs: Lignin Modifying Enzymes LRET: Long Range Electron Transfer MEGA: Molecular Evolutionary Genetics Analysis MCO: Multicopper
Recommended publications
  • Pseudomonas Spp. and Other Psychrotrophic

    Pseudomonas Spp. and Other Psychrotrophic

    Pesq. Vet. Bras. 39(10):807-815, October 2019 DOI: 10.1590/1678-5150-PVB-6037 Original Article Livestock Diseases ISSN 0100-736X (Print) ISSN 1678-5150 (Online) PVB-6037 LD Pseudomonas spp. and other psychrotrophic microorganisms in inspected and non-inspected Brazilian Minas Frescal cheese: proteolytic, lipolytic and AprX production potential1 Pedro I. Teider Junior2, José C. Ribeiro Júnior3* , Eric H. Ossugui2, Ronaldo Tamanini2, Juliane Ribeiro2, Gislaine A. Santos2 2 and Vanerli Beloti2 , Amauri A. Alfieri ABSTRACT.- Teider Junior P.I., Ribeiro Júnior J.C., Ossugui E.H., Tamanini R., Ribeiro J., Santos G.A., Pseudomonas spp. and other psychrotrophic microorganisms Pseudomonas spp. and other psychrotrophic in inspected and non-inspected Brazilian Minas Frescal cheese: proteolytic, lipolytic andAlfieri AprX A.A. production& Beloti V. 2019. potential . Pesquisa Veterinária Brasileira 39(10):807-815. Instituto microorganisms in inspected and non- Nacional de Ciência e Tecnologia para a Cadeia Produtiva do Leite, Universidade Estadual de inspected Brazilian Minas Frescal cheese: Londrina, Rodovia Celso Garcia Cid PR-445 Km 380, Cx. Postal 10.011, Campus Universitário, proteolytic, lipolytic and AprX production Londrina, PR 86057-970, Brazil. E-mail: [email protected] The most consumed cheese in Brazil, Minas Frescal cheese (MFC) is highly susceptible to potential microbial contamination and clandestine production and commercialization can pose a risk to consumer health. The storage of this fresh product under refrigeration, although more appropriate, may favor the growth of spoilage psychrotrophic bacteria. The objective of this [Pseudomonas spp. e outros micro-organismos study was to quantify and compare Pseudomonas spp. and other psychrotrophic bacteria in inspected and non-inspected MFC samples, evaluate their lipolytic and proteolytic activities and e não inspecionados: potencial proteolítico, lipolítico e their metalloprotease production potentials.
  • Succession and Persistence of Microbial Communities and Antimicrobial Resistance Genes Associated with International Space Stati

    Succession and Persistence of Microbial Communities and Antimicrobial Resistance Genes Associated with International Space Stati

    Singh et al. Microbiome (2018) 6:204 https://doi.org/10.1186/s40168-018-0585-2 RESEARCH Open Access Succession and persistence of microbial communities and antimicrobial resistance genes associated with International Space Station environmental surfaces Nitin Kumar Singh1, Jason M. Wood1, Fathi Karouia2,3 and Kasthuri Venkateswaran1* Abstract Background: The International Space Station (ISS) is an ideal test bed for studying the effects of microbial persistence and succession on a closed system during long space flight. Culture-based analyses, targeted gene-based amplicon sequencing (bacteriome, mycobiome, and resistome), and shotgun metagenomics approaches have previously been performed on ISS environmental sample sets using whole genome amplification (WGA). However, this is the first study reporting on the metagenomes sampled from ISS environmental surfaces without the use of WGA. Metagenome sequences generated from eight defined ISS environmental locations in three consecutive flights were analyzed to assess the succession and persistence of microbial communities, their antimicrobial resistance (AMR) profiles, and virulence properties. Metagenomic sequences were produced from the samples treated with propidium monoazide (PMA) to measure intact microorganisms. Results: The intact microbial communities detected in Flight 1 and Flight 2 samples were significantly more similar to each other than to Flight 3 samples. Among 318 microbial species detected, 46 species constituting 18 genera were common in all flight samples. Risk group or biosafety level 2 microorganisms that persisted among all three flights were Acinetobacter baumannii, Haemophilus influenzae, Klebsiella pneumoniae, Salmonella enterica, Shigella sonnei, Staphylococcus aureus, Yersinia frederiksenii,andAspergillus lentulus.EventhoughRhodotorula and Pantoea dominated the ISS microbiome, Pantoea exhibited succession and persistence. K. pneumoniae persisted in one location (US Node 1) of all three flights and might have spread to six out of the eight locations sampled on Flight 3.
  • Deconstruction of Lignin: from Enzymes to Microorganisms

    Deconstruction of Lignin: from Enzymes to Microorganisms

    molecules Review Deconstruction of Lignin: From Enzymes to Microorganisms Jéssica P. Silva 1, Alonso R. P. Ticona 1 , Pedro R. V. Hamann 1, Betania F. Quirino 2 and Eliane F. Noronha 1,* 1 Enzymology Laboratory, Cell Biology Department, University of Brasilia, 70910-900 Brasília, Brazil; [email protected] (J.P.S.); [email protected] (A.R.P.T.); [email protected] (P.R.V.H.) 2 Genetics and Biotechnology Laboratory, Embrapa-Agroenergy, 70770-901 Brasília, Brazil; [email protected] * Correspondence: [email protected]; Tel.: +55-61-3307-2152 Abstract: Lignocellulosic residues are low-cost abundant feedstocks that can be used for industrial applications. However, their recalcitrance currently makes lignocellulose use limited. In natural environments, microbial communities can completely deconstruct lignocellulose by synergistic action of a set of enzymes and proteins. Microbial degradation of lignin by fungi, important lignin degraders in nature, has been intensively studied. More recently, bacteria have also been described as able to break down lignin, and to have a central role in recycling this plant polymer. Nevertheless, bacterial deconstruction of lignin has not been fully elucidated yet. Direct analysis of environmental samples using metagenomics, metatranscriptomics, and metaproteomics approaches is a powerful strategy to describe/discover enzymes, metabolic pathways, and microorganisms involved in lignin breakdown. Indeed, the use of these complementary techniques leads to a better understanding of the composition, function, and dynamics of microbial communities involved in lignin deconstruction. We focus on omics approaches and their contribution to the discovery of new enzymes and reactions that impact the development of lignin-based bioprocesses.
  • Oxidative Degradation of Non-Phenolic Lignin During Lipid Peroxidation by Fungal Manganese Peroxidase

    Oxidative Degradation of Non-Phenolic Lignin During Lipid Peroxidation by Fungal Manganese Peroxidase

    FEBS Letters 354 (1994) 297-300 FEBS 14759 Oxidative degradation of non-phenolic lignin during lipid peroxidation by fungal manganese peroxidase Wuli Bao, Yaichi Fukushima, Kenneth A. Jensen Jr., Mark A. Moen, Kenneth E. Hammel* USDA Forest Products Laboratory, Madison, WI 53705, USA Received 3 October 1994 Abstract A non-phenolic lignin model dimer, 1-(4-ethoxy-3-methoxyphenyl)-2-phenoxypropane-l ,3-diol, was oxidized by a lipid peroxidation system that consisted of a fungal manganese peroxidase, Mn(II), and unsaturated fatty acid esters. The reaction products included 1-(4-ethoxy-3- methoxyphenyl)-1-oxo-2-phenoxy-3-hydroxypropane and 1-(4-ethoxy-3-methoxyphenyl)- 1-oxo-3-hydroxypropane, indicating that substrate oxida- tion occurred via benzylic hydrogen abstraction. The peroxidation system depolymerized both exhaustively methylated (non-phenolic) and unmeth- ylated (phenolic) synthetic lignins efficiently. It may therefore enable white-rot fungi to accomplish the initial delignification of wood. Key words: Manganese peroxidase; Lipid peroxidation; Ligninolysis; Non-phenolic lignin; White-rot fungus 1. Introduction 2. Materials and methods White-rot fungi have evolved unique ligninolytic mecha- 2.1. Reagents l-(4-Ethoxy-3-methoxyphenyl)-2-phenoxypropane-l,3-diol (I) [12] nisms, which enable them to play an essential role in terrestrial 1-(4-ethoxy-3-methoxyphenyl)-l-oxo-2-phenoxy-3-hydroxypropane ecosystems by degrading and recycling lignified biomass. The (II) [13], and l-(4-ethoxy-3-methoxyphenyl)-l-oxo-3-hydroxypropane chemical recalcitrance, random structure, and large size of lig- (III) [14] were prepared by the indicated methods.I labeled with 14C at Cl (0.066 mCi· mmol-1) was prepared in the same manner as the unla- nin require that these mechanisms be oxidative, non-specific, 14 beled compound, using [1- C]acetic acid as the labeled precursor.
  • Neonatal Septicemia Caused by a Rare Pathogen: Raoultella Planticola

    Neonatal Septicemia Caused by a Rare Pathogen: Raoultella Planticola

    Chen et al. BMC Infectious Diseases (2020) 20:676 https://doi.org/10.1186/s12879-020-05409-5 CASE REPORT Open Access Neonatal septicemia caused by a rare pathogen: Raoultella planticola - a report of four cases Xianrui Chen1,2,3, Shaoqing Guo1,2,3* , Dengli Liu1,2,3 and Meizhen Zhong1,2,3 Abstract Background: Raoultella planticola(R.planticola) is a very rare opportunistic pathogen and sometimes even associated with fatal infection in pediatric cases. Recently,the emergence of carbapenem resistance strains are constantly being reported and a growing source of concern for pediatricians. Case presentation: We reported 4 cases of neonatal septicemia caused by Raoultella planticola. Their gestational age was 211 to 269 days, and their birth weight was 1490 to 3000 g.The R. planticola infections were detected on the 9th to 27th day after hospitalizationandoccuredbetweenMayandJune.They clinically manifested as poor mental response, recurrent cyanosis, apnea, decreased heart rate and blood oxygen, recurrent jaundice, fever or nonelevation of body temperature. The C-reactive protein and procalcitonin were elevated at significantly in the initial phase of the infection,and they had leukocytosis or leukopenia. Prior to R.planticola infection,all of them recevied at least one broad-spectrum antibiotic for 7- 27d.All the R.planticola strains detected were only sensitive to amikacin, but resistant to other groups of drugs: cephalosporins (such as cefazolin, ceftetan,etc) and penicillins (such as ampicillin-sulbactam,piperacillin, etc),and even developed resistance to carbapenem. All the infants were clinically cured and discharged with overall good prognosis. Conclusion: Neonatal septicemia caused by Raoultella planticola mostly occured in hot and humid summer, which lack specific clinical manifestations.
  • Bioresources.Com

    Bioresources.Com

    PEER-REVIEWED ARTICLE bioresources.com HYPERPRODUCTIVITY OF EXTRACELLULAR ENZYMES FROM INDIGENOUS WHITE ROT FUNGI (P. chrysosporium IBL-03) BY UTILIZING AGRO-WASTES Muhammad Asgher, Nadeem Ahmed, and Hafiz Muhammad Nasir Iqbal* An indigenous locally isolated white rot fungal strain Phanerochaete chrysosporium IBL-03 was investigated for the hyper-production of ligninolytic enzymes from different agro-industrial wastes including wheat straw, rice straw, banana stalks, corncobs, corn stover, and sugarcane bagasse as substrate material in still culture fermentation technique. Screening experiments were performed at 30oC from 1 to 10 days and maximum enzyme activities were recorded after the 5th day of incubation on banana stalk. P. chrysosporium IBL-03 produced highest activities of lignin peroxidase (LiP) and manganese peroxidase (MnP) but no laccase activity was detected in any fermented culture media. Production of ligninolytic enzymes was substantially enhanced through the optimization process. When banana stalk at 66.6 % moisture level and pH 4.5 was inoculated with 5mL spore suspension of P. chrysosporium IBL-03 at 35oC in the presence of molasses (1%) as carbon source, ammonium sulfate (0.2%) as nitrogen supplement, (1%) Tween-80 (0.3 mL) as surfactant and mediators (MnSO4 and veratryl alcohol) enhanced the LiP and MnP production up to 1040 and 965 (U/mL), respectively. Keywords: Phanerochaete chrysosporium IBL-03; Extracellular enzymes; Agro-wastes; SSF; Optimization Contact information: Department of Chemistry and Biochemistry, University of Agriculture, Faisalabad Pakistan; * Corresponding Author: Telephone# +92-307-6715243 E-mail: [email protected] INTRODUCTION White rot fungi (WRF) are among the most robust micro-organisms, having the ability to degrade the major components of lignocellulosic sources, cellulose, hemicelluloses, and lignin as available hydrolyzable nutrients efficiently through their nonspecific and non stereo-selective extracellular enzyme system (Papinutti and Forchiassin 2007; Ruhl et al.
  • CTX-M-9 Group ESBL-Producing Raoultella Planticola Nosocomial

    CTX-M-9 Group ESBL-Producing Raoultella Planticola Nosocomial

    Tufa et al. Ann Clin Microbiol Antimicrob (2020) 19:36 https://doi.org/10.1186/s12941-020-00380-0 Annals of Clinical Microbiology and Antimicrobials CASE REPORT Open Access CTX-M-9 group ESBL-producing Raoultella planticola nosocomial infection: frst report from sub-Saharan Africa Tafese Beyene Tufa1,2,3*† , Andre Fuchs2,3†, Torsten Feldt2,3, Desalegn Tadesse Galata1, Colin R. Mackenzie4, Klaus Pfefer4 and Dieter Häussinger2,3 Abstract Background: Raoultella are Gram-negative rod-shaped aerobic bacteria which grow in water and soil. They mostly cause nosocomial infections associated with surgical procedures. This case study is the frst report of a Raoultella infec- tion in Africa. Case presentation We report a case of a surgical site infection (SSI) caused by Raoultella planticola which developed after caesarean sec- tion (CS) and surgery for secondary small bowel obstruction. The patient became febrile with neutrophilia (19,157/µL) 4 days after laparotomy and started to develop clinical signs of a SSI on the 8 th day after laparotomy. The patient con- tinued to be febrile and became critically ill despite empirical treatment with ceftriaxone and vancomycin. Raoultella species with extended antimicrobial resistance (AMR) carrying the CTX-M-9 β-lactamase was isolated from the wound discharge. Considering the antimicrobial susceptibility test, ceftriaxone was replaced by ceftazidime. The patient recovered and could be discharged on day 29 after CS. Conclusions: Raoultella planticola was isolated from an infected surgical site after repeated abdominal surgery. Due to the infection the patient’s stay in the hospital was prolonged for a total of 4 weeks. It is noted that patients under- going surgical and prolonged inpatient treatment are at risk for infections caused by Raoultella.
  • Kinetic Approaches to Measuring Peroxiredoxin Reactivity

    Kinetic Approaches to Measuring Peroxiredoxin Reactivity

    Mol. Cells 2016; 39(1): 26-30 http://dx.doi.org/10.14348/molcells.2016.2325 Molecules and Cells http://molcells.org Established in 1990 Kinetic Approaches to Measuring Peroxiredoxin Reactivity Christine C. Winterbourn*, and Alexander V. Peskin Peroxiredoxins are ubiquitous thiol proteins that catalyse demonstrated surprisingly low reactivity with thiol reagents such the breakdown of peroxides and regulate redox activity in as iodoacetamide and other oxidants such as chloramines the cell. Kinetic analysis of their reactions is required in (Peskin et al., 2007) and it is clear that the low pKa of the active order to identify substrate preferences, to understand how site thiol is insufficient to confer the high peroxide reactivity. In molecular structure affects activity and to establish their fact, typical low molecular weight and protein thiolates react -1 -1 physiological functions. Various approaches can be taken, with H2O2 with a rate constant of 20 M s whereas values of including the measurement of rates of individual steps in Prxs are 105-106 fold higher (Winterbourn and Hampton, 2008). the reaction pathway by stopped flow or competitive kinet- An elegant series of structural and mutational studies (Hall et al., ics, classical enzymatic analysis and measurement of pe- 2010; Nakamura et al., 2010; Nagy et al., 2011) have shown roxidase activity. Each methodology has its strengths and that to get sufficient rate enhancement, it is necessary to acti- they can often give complementary information. However, vate the peroxide. As discussed in detail elsewhere (Hall et al., it is important to understand the experimental conditions 2010; 2011), this involves formation of a transition state in of the assay so as to interpret correctly what parameter is which hydrogen bonding of the peroxide to conserved Arg and being measured.
  • Prokaryotic Origins of the Non-Animal Peroxidase Superfamily and Organelle-Mediated Transmission to Eukaryotes

    Prokaryotic Origins of the Non-Animal Peroxidase Superfamily and Organelle-Mediated Transmission to Eukaryotes

    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Genomics 89 (2007) 567–579 www.elsevier.com/locate/ygeno Prokaryotic origins of the non-animal peroxidase superfamily and organelle-mediated transmission to eukaryotes Filippo Passardi a, Nenad Bakalovic a, Felipe Karam Teixeira b, Marcia Margis-Pinheiro b,c, ⁎ Claude Penel a, Christophe Dunand a, a Laboratory of Plant Physiology, University of Geneva, Quai Ernest-Ansermet 30, CH-1211 Geneva 4, Switzerland b Department of Genetics, Institute of Biology, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil c Department of Genetics, Federal University of Rio Grande do Sul, Rio Grande do Sul, Brazil Received 16 June 2006; accepted 18 January 2007 Available online 13 March 2007 Abstract Members of the superfamily of plant, fungal, and bacterial peroxidases are known to be present in a wide variety of living organisms. Extensive searching within sequencing projects identified organisms containing sequences of this superfamily. Class I peroxidases, cytochrome c peroxidase (CcP), ascorbate peroxidase (APx), and catalase peroxidase (CP), are known to be present in bacteria, fungi, and plants, but have now been found in various protists. CcP sequences were detected in most mitochondria-possessing organisms except for green plants, which possess only ascorbate peroxidases. APx sequences had previously been observed only in green plants but were also found in chloroplastic protists, which acquired chloroplasts by secondary endosymbiosis. CP sequences that are known to be present in prokaryotes and in Ascomycetes were also detected in some Basidiomycetes and occasionally in some protists.
  • Bioresources.Com

    Bioresources.Com

    PEER-REVIEWED REVIEW ARTICLE bioresources.com BIOLOGICAL PRETREATMENT OF LIGNOCELLULOSES WITH WHITE-ROT FUNGI AND ITS APPLICATIONS: A REVIEW a,b c, d Isroi, Ria Millati, * Siti Syamsiah, Claes Niklasson,b Muhammad Nur Cahyanto,c f Knut Lundquist,e and Mohammad J. Taherzadeh Lignocellulosic carbohydrates, i.e. cellulose and hemicellulose, have abundant potential as feedstock for production of biofuels and chemicals. However, these carbohydrates are generally infiltrated by lignin. Breakdown of the lignin barrier will alter lignocelluloses structures and make the carbohydrates accessible for more efficient bioconversion. White-rot fungi produce ligninolytic enzymes (lignin peroxidase, manganese peroxidase, and laccase) and efficiently mineralise lignin into CO2 and H2O. Biological pretreatment of lignocelluloses using white-rot fungi has been used for decades for ruminant feed, enzymatic hydrolysis, and biopulping. Application of white-rot fungi capabilities can offer environmentally friendly processes for utilising lignocelluloses over physical or chemical pretreatment. This paper reviews white-rot fungi, ligninolytic enzymes, the effect of biological pretreatment on biomass characteristics, and factors affecting biological pretreatment. Application of biological pretreatment for enzymatic hydrolysis, biofuels (bioethanol, biogas and pyrolysis), biopulping, biobleaching, animal feed, and enzymes production are also discussed. Keywords: Biological pretreatment; White-rot fungi; Lignocellulose; Solid-state fermentation; Lignin peroxidase;
  • Textile Dye Biodecolorization by Manganese Peroxidase: a Review

    Textile Dye Biodecolorization by Manganese Peroxidase: a Review

    molecules Review Textile Dye Biodecolorization by Manganese Peroxidase: A Review Yunkang Chang 1,2, Dandan Yang 2, Rui Li 2, Tao Wang 2,* and Yimin Zhu 1,* 1 Institute of Environmental Remediation, Dalian Maritime University, Dalian 116026, China; [email protected] 2 The Lab of Biotechnology Development and Application, School of Biological Science, Jining Medical University, No. 669 Xueyuan Road, Donggang District, Rizhao 276800, China; [email protected] (D.Y.); [email protected] (R.L.) * Correspondence: [email protected] (T.W.); [email protected] (Y.Z.); Tel.: +86-063-3298-3788 (T.W.); +86-0411-8472-6992 (Y.Z.) Abstract: Wastewater emissions from textile factories cause serious environmental problems. Man- ganese peroxidase (MnP) is an oxidoreductase with ligninolytic activity and is a promising biocatalyst for the biodegradation of hazardous environmental contaminants, and especially for dye wastewater decolorization. This article first summarizes the origin, crystal structure, and catalytic cycle of MnP, and then reviews the recent literature on its application to dye wastewater decolorization. In addition, the application of new technologies such as enzyme immobilization and genetic engineering that could improve the stability, durability, adaptability, and operating costs of the enzyme are highlighted. Finally, we discuss and propose future strategies to improve the performance of MnP-assisted dye decolorization in industrial applications. Keywords: manganese peroxidase; biodecolorization; dye wastewater; immobilization; recombi- nant enzyme Citation: Chang, Y.; Yang, D.; Li, R.; Wang, T.; Zhu, Y. Textile Dye Biodecolorization by Manganese Peroxidase: A Review. Molecules 2021, 26, 4403. https://doi.org/ 1. Introduction 10.3390/molecules26154403 The textile industry produces large quantities of wastewater containing different types of dyes used during the dyeing process, which cause great harm to the environment [1,2].
  • Severe Pansinusitis Due to Raoultella Ornithinolytica

    Severe Pansinusitis Due to Raoultella Ornithinolytica

    American Journal of Infectious Diseases Case Report Severe Pansinusitis Due to Raoultella Ornithinolytica Mitchell R. Gore Department of Otolaryngology, State University of New York-Upstate Medical University, Syracuse, NY, USA Article history Abstract: Raoultella ornithinolytica is a gram -negative aerobic bacterium Received: 23-09-2017 typically found in plants, soil and water. Reports of Raoultella Revised: 05-12-2017 ornithinolytica causing infections in humans, especially in the head and Accepted: 20-12-2017 neck, are rare. Herein we report a case of a woman with severe septal deviation, chronic headaches and facial pain who was revealed to have Tel: +1 315 492 3741 Fax: +1 315 492 5791 Raoultella ornithinolytica pansinusitis incidentally noted during an Email: [email protected] endoscopic septoplasty. Raoultella ornithinolytica was isolated from cultures of the diffuse purulent drainage found in her maxillary and ethmoid sinuses. This case indicates that while a rare cause of head and neck infection in humans, Raoultella ornithinolytica can be found as the causative pathogen in severe sinusitis. Keywords: Raoultella ornithinolytica , Sinusitis, Infection Introduction distress. Head and neck and cranial nerve examinations were normal. Nasal endoscopy revealed severe bilateral Raoultella ornithinolytica is a member of a genus of inferior turbinate hypertrophy and severe septal deviation Gram-negative, oxidase-negative, aerobic, nonmotile, causing bilateral nasal obstruction. The inferior turbinate capsulated, facultatively anaerobic rods closely related to hypertrophy and septal deviation were so significant that the Klebsiella genus in the Enterobacteriaceae family. the middle meatus could not be visualized. Given the The genus is named after noted French bacteriologist patient’s complaints she was counseled on the risks, Didier Raoult (Drancourt et al.