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Lantibiotic Nisin and Its Detection Methods

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Lantibiotic Nisin and Its Detection Methods View metadata,citationandsimilarpapersatcore.ac.uk Recent Publications in this Series: LantibioticNisinandItsDetectionMethods JUSTUS REUNANEN 10/2007 Jenni Antikainen Surface Proteins of Lactobacillus crispatus: Adhesive Properties and Cell Wall Anchoring 11/2007 Jing Li Novel Molecular Mechanisms of Arabidopsis Disease Resistance 12/2007 Piia Salo Thin-Layer Chromatography with Ultraviolet and Mass Spectrometric Detection: From Preparative-Layer to Miniaturized Ultra-Thin-Layer Technique 13/2007 Mikko Sairanen Neurotrophins and Neuronal Plasticity in the Action of Antidepressants and Morphine 14/2007 Camilla Ribacka Redox-linked Proton Transfer by Cytochrome C Oxidase 15/2007 Päivi Ramu Outer Membrane Protease/adhesin PgtE of S. enterica: Role in Salmonella-Host Interaction 16/2007 Joni Alvesalo Drug Discovery Screening and the Application of Genomics and Proteomics in the Drug Development Process for Chlamydia pneumoniae 17/2007 Tomi Jukkola FGFR1 Regulated Gene-Expression, Cell Proliferation and Differentiation in the Developing Midbrain and Hindbrain 18/2007 Maarit Hellman Structural Characteristics Affecting Functions of Two Actin Regulating Proteins 19/2007 Rasa Gabrenaite-Verkhovskaya Movement-Associated Proteins of Potato Virus A: Attachment to Virus Particles and Phosphorylation 20/2007 Henna Vihola Studies on Thermosensitive Poly(N-Vinylcaprolactam) Based Polymers for Pharmaceutical Applications 21/2007 Terhi Hakala Characterization of the Lignin-Modifying Enzymes of the Selective White-Rot Fungus Physisporinus Rivulosus Lantibiotic Nisin and Its Detection Methods 22/2007 Ilya Belevich Proton Translocation Coupled to Electron Transfer Reactions in Terminal Oxidases 23/2007 Johan Pahlberg Spectral Tuning and Adaptation to Different Light Environments of Mysid Visual Pigments 24/2007 Beata Kluczek-Turpeinen Lignocellulose Degradation and Humus Modifi cation by the Fungus Paecilomyces infl atus 25/2007 Sabiruddin Mirza JUSTUS REUNANEN Crystallization as a Tool for Controlling and Designing Properties of Pharmaceutical Solids 26/2007 Kaisa Marjamaa Peroxidases in Lignifying Xylem of Norway Spruce, Scots Pine and Silver Birch 27/2007 Pekka Nieminen Department of Applied Chemistry and Microbiology Molecular Genetics of Tooth Agenesis 28/2007 Sanna Koutaniemi Division of Microbiology Lignin Biosynthesis in Norway Spruce: from a Model System to the Tree Faculty of Agriculture and Forestry 29/2007 Anne Rantala Evolution and Detection of Cyanobacterial Hepatotoxin Synthetase Genes and 30/2007 Tiina Sikanen SU-8-Based Microchips for Capillary Electrophoresis and Electrospray Ionization Mass Spectrometry Viikki Graduate School in Biosciences 31/2007 Pieta Mattila University of Helsinki Missing-In-Metastasis (MIM)Regulates Cell Morphology by Promoting Plasma Membrane and Actin Cytoskeleton Dynamics Helsinki 2007 ISSN 1795-7079 ISBN 978-952-10-4435-9provided by Dissertationes bioscientiarum molecularium Universitatis Helsingiensis in Viikki 32/2007 Helsingin yliopistondigitaalinenarkisto brought toyouby 32/2007 CORE Division of Microbiology Department of Applied Chemistry and Microbiology University of Helsinki Finland Lantibiotic nisin and its detection methods Justus Reunanen ACADEMIC DISSERTATION To be presented, with the permission of the Faculty of Agriculture and Forestry of the University of Helsinki, for public examination in lecture room 5, at the University of Helsinki, B-building, Latokartanonkaari 7, on December 14th 2007, at 12 noon. Helsinki 2007 Supervisor: Professor Per Saris Department of Applied Chemistry and Microbiology University of Helsinki Finland Reviewers: Professor Matti Karp Institute of Environmental Engineering and Biotechnology Tampere University of Technology Finland Professor Martin Romantschuk Department of Ecological and Environmental Sciences University of Helsinki Finland Opponent: PhD Paul Ross Moorepark Food Research Centre Teagasc, Ireland ISSN 1795-7079 ISBN 978-952-10-4435-9 (pbk.) ISBN 978-952-10-4436-6 (PDF) e-mail: justus.reunanen@helsinki.fi Edita Prima Oy Helsinki 2007 Front cover picture: Author’s desk Abstract The type A lantibiotic nisin produced by several Lactococcus lactis strains, and one Streptococcus uberis strainis a small antimicrobial peptide that inhibits the growth of a wide range of gram-positive bacteria, such as Bacillus, Clostridium, Listeria and Staphylococcus species. It is nontoxic to humans and used as a food preservative (E234) in more than 50 countries including the EU, the USA, and China. National legislations concerning maximum addition levels of nisin in different foods vary greatly. Therefore, there is a demand for non-laborious and sensitive methods to identify and quantify nisin reliably from different food matrices. The horizontal inhibition assay, based on the inhibitory effect of nisin to Micrococcus luteus is the base for most quantification methods developed so far. However, the sensitivity and accuracy of the agar diffusion method is affected by several parameters. Immunological tests have also been described. Taken into account the sensitivity of immunological methods to interfering substances within sample matrices, and possible cross-reactivities with lantibiotics structurally close to nisin, their usefulness for nisin detection from food samples remains limited. The proteins responsible for nisin biosynthesis, and producer self-immunity are encoded by genes arranged into two inducible operons, nisA/Z/QBTCIPRK and nisFEG, which also contain internal, constitutive promoters PnisI and PnisR. The transmembrane histidine kinase NisK and the response regulator NisR form a two-component signal transduction system, in which NisK autophosphorylates after exposure to extra cellular nisin, and subsequently transfers the phosphate to NisR. The phosphorylated NisR then relays the signal downstream by binding to two regulated promoters in the nisin gene cluster, i.e the nisA/Z/Qand the nisF promoters, thus activating transcription of the structural gene nisA/Z/Q and the downstream genes nisBTCIPRK from the nisA/Z/Q promoter, and the genes nisFEG from the nisF promoter. In this work two novel and highly sensitive nisin bioassays were developed. Both of these quantifi cation methods were based on NisRK mediated, nisin induced Green Fluorescent Protein (GFP) fl uorescence. The suitabilities of these assays for quantifi ca- tion of nisin from food samples were evaluated in several food matrices. These bioassays had nisin sensitivities in the nanogram or picogram levels. In addition, shelf life of nisin in cooked sausages and retainment of the induction activity of nisin in intestinal chyme (intestinal content) was assessed. Contents Abstract List of original publications ......................................................................................... 5 Abbreviations .............................................................................................................. 6 Review of the literature ............................................................................................... 7 1. Bacteriocins ......................................................................................................... 7 1.1 Bacteriocins produced by lactic acid bacteria ................................................ 7 1.2 Lantibiotics .................................................................................................... 7 2 Nisin ....................................................................................................................10 2.1 Structure and chemical characteristics ......................................................... 11 2.1.1 Primary structure ................................................................................. 11 2.1.2 Three dimensional structure ................................................................ 11 2.2 Nisin genes and biosynthesis of nisin .......................................................... 13 2.2.1 Nisin regulon ....................................................................................... 14 2.2.2 NisB .................................................................................................... 14 2.2.3 NisC .................................................................................................... 15 2.2.4 NisT..................................................................................................... 15 2.2.5 NisP ..................................................................................................... 16 2.2.6 Regulation of biosynthesis .................................................................. 17 2.3 Antimicrobial mechanisms .......................................................................... 18 2.4 Immunity ..................................................................................................... 20 2.5 Detection methods ....................................................................................... 22 2.5.1 International nisin activity unit, IU .................................................... 22 2.5.2 Chemical methods .............................................................................. 22 2.5.3 Methods based on growth inhibition ................................................. 23 2.5.3.1 Methods with liquid media ..................................................... 23 2.5.3.2 Methods with solid media .................................................... 23 2.5.4 Immunological methods ..................................................................... 25 2.5.5 Other methods
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