Mpev Is the Lyase Isomerase for the Doubly-Linked Phycourobilin On
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Ecological and Physiological Studies on Freshwater Autotrophic Picoplankton
Durham E-Theses Ecological and physiological studies on freshwater autotrophic picoplankton Hawley, Graham R.W. How to cite: Hawley, Graham R.W. (1990) Ecological and physiological studies on freshwater autotrophic picoplankton, Durham theses, Durham University. Available at Durham E-Theses Online: http://etheses.dur.ac.uk/6058/ Use policy The full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that: • a full bibliographic reference is made to the original source • a link is made to the metadata record in Durham E-Theses • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders. Please consult the full Durham E-Theses policy for further details. Academic Support Oce, Durham University, University Oce, Old Elvet, Durham DH1 3HP e-mail: [email protected] Tel: +44 0191 334 6107 http://etheses.dur.ac.uk Ecological and physiological studies on freshwater autotrophic picoplankton by Graham R.W. Hawley B.Sc. (DI.melm) A thesis submdtted for the degree of Doctor of Philosophy in the university of Durham, England. Department of Biological Sciences, August 1990 The copyright of this thesis rests with the author. No quotation from it should be published without his prior written consent and information derived from it should be acknowledged. w~ 1 8 AUG 1992 2 This thesis is entirely the result of my~~ work. -
UNIVERSITY of CALIFORNIA, SAN DIEGO Indicators of Iron
UNIVERSITY OF CALIFORNIA, SAN DIEGO Indicators of Iron Metabolism in Marine Microbial Genomes and Ecosystems A dissertation submitted in partial satisfaction of the requirements for the degree Doctor of Philosophy in Oceanography by Shane Lahman Hogle Committee in charge: Katherine Barbeau, Chair Eric Allen Bianca Brahamsha Christopher Dupont Brian Palenik Kit Pogliano 2016 Copyright Shane Lahman Hogle, 2016 All rights reserved . The Dissertation of Shane Lahman Hogle is approved, and it is acceptable in quality and form for publication on microfilm and electronically: Chair University of California, San Diego 2016 iii DEDICATION Mom, Dad, Joel, and Marie thank you for everything iv TABLE OF CONTENTS Signature Page ................................................................................................................... iii Dedication .......................................................................................................................... iv Table of Contents .................................................................................................................v List of Figures ................................................................................................................... vii List of Tables ..................................................................................................................... ix Acknowledgements ..............................................................................................................x Vita .................................................................................................................................. -
Scholarworks@UNO
University of New Orleans ScholarWorks@UNO University of New Orleans Theses and Dissertations Dissertations and Theses Summer 8-4-2011 Identification and characterization of enzymes involved in the biosynthesis of different phycobiliproteins in cyanobacteria Avijit Biswas University of New Orleans, [email protected] Follow this and additional works at: https://scholarworks.uno.edu/td Part of the Biochemistry, Biophysics, and Structural Biology Commons Recommended Citation Biswas, Avijit, "Identification and characterization of enzymes involved in the biosynthesis of different phycobiliproteins in cyanobacteria" (2011). University of New Orleans Theses and Dissertations. 446. https://scholarworks.uno.edu/td/446 This Dissertation-Restricted is protected by copyright and/or related rights. It has been brought to you by ScholarWorks@UNO with permission from the rights-holder(s). You are free to use this Dissertation-Restricted in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s) directly, unless additional rights are indicated by a Creative Commons license in the record and/or on the work itself. This Dissertation-Restricted has been accepted for inclusion in University of New Orleans Theses and Dissertations by an authorized administrator of ScholarWorks@UNO. For more information, please contact [email protected]. Identification and characterization of enzymes involved in biosynthesis of different phycobiliproteins in cyanobacteria A Thesis Submitted to the Graduate Faculty of the University of New Orleans in partial fulfillment of the requirements for the degree of Doctor of Philosophy In Chemistry (Biochemistry) By Avijit Biswas B.S. -
Extractuion, Partial Pirificatuon and Anti
J. Algal Biomass Utln. 2012, 3 (3): 7– 11 Purification, and antibacterial activity of phycocyanin from Spirulina © PHYCO SPECTRUM INC Extraction, partial purification, and antibacterial activity of phycocyanin from Spirulina isolated from fresh water body against various human pathogens M. Muthulakshmi, A. Saranya, M. Sudha, and G. Selvakumar* Department of Microbiology and Biochemistry, Nadar Saraswathi College of Arts & Science, Theni 625531, Tamil Nadu, India *Department of Microbiology, Department of Distance Education, Alagappa University, Karaikudi, Tamil Nadu, India ABSTRACT The phycobilin pigments are intensively fluorescence and water soluble. They are categorized into three types: pigments containing high energies (phycoerythrins), intermediate energies (phycocyanins), and low energies (allophycocyanins). Among them, crude-phycocyanin (c-pc) has been considered to be the most preferred one. The present study was undertaken to evaluate the antibacterial activity of c-pc which was isolated from the blue green algae Spirulina platensis. C-pc was extracted by sonication, followed by centrifugation and filtration. The crude form of phycocyanin was purified by ammonium sulphate precipitation, membrane filtration, and dialysis method. Antibacterial activities were obtained from various human pathogens. The results showed that all Spirulina maxima extracts exhibited great potential antibacterial activities against five bacterial strains with inhibition zones of range 7–13 mm. Key words: Spirulina maxima, c-phycocyanin, antibacterial activity INTRODUCTION the cells enclosed in a thin sheath. Spirulina has a Microalgae are a very diverse group of organisms very long history of being served as a source of food that consist of both prokaryotic and eukaryotic for human being. forms. Although most microalgae are phototropic some species are also capable of showing Spirulina is a spiral filament generally found in heterotrophic growth. -
Scalable Production of Biliverdin Ixα by Escherichia Coli Dong Chen1, Jason D Brown1, Yukie Kawasaki2, Jerry Bommer3 and Jon Y Takemoto1,2*
Chen et al. BMC Biotechnology 2012, 12:89 http://www.biomedcentral.com/1472-6750/12/89 RESEARCH ARTICLE Open Access Scalable production of biliverdin IXα by Escherichia coli Dong Chen1, Jason D Brown1, Yukie Kawasaki2, Jerry Bommer3 and Jon Y Takemoto1,2* Abstract Background: Biliverdin IXα is produced when heme undergoes reductive ring cleavage at the α-methene bridge catalyzed by heme oxygenase. It is subsequently reduced by biliverdin reductase to bilirubin IXα which is a potent endogenous antioxidant. Biliverdin IXα, through interaction with biliverdin reductase, also initiates signaling pathways leading to anti-inflammatory responses and suppression of cellular pro-inflammatory events. The use of biliverdin IXα as a cytoprotective therapeutic has been suggested, but its clinical development and use is currently limited by insufficient quantity, uncertain purity, and derivation from mammalian materials. To address these limitations, methods to produce, recover and purify biliverdin IXα from bacterial cultures of Escherichia coli were investigated and developed. Results: Recombinant E. coli strains BL21(HO1) and BL21(mHO1) expressing cyanobacterial heme oxygenase gene ho1 and a sequence modified version (mho1) optimized for E. coli expression, respectively, were constructed and shown to produce biliverdin IXα in batch and fed-batch bioreactor cultures. Strain BL21(mHO1) produced roughly twice the amount of biliverdin IXα than did strain BL21(HO1). Lactose either alone or in combination with glycerol supported consistent biliverdin IXα production by strain BL21(mHO1) (up to an average of 23. 5mg L-1 culture) in fed-batch mode and production by strain BL21 (HO1) in batch-mode was scalable to 100L bioreactor culture volumes. -
Adaptation to Blue Light in Marine Synechococcus Requires Mpeu, an Enzyme with Similarity to Phycoerythrobilin Lyase Isomerases
University of New Orleans ScholarWorks@UNO Biological Sciences Faculty Publications Department of Biological Sciences 2-21-2017 Adaptation to Blue Light in Marine Synechococcus Requires MpeU, an Enzyme with Similarity to Phycoerythrobilin Lyase Isomerases Wendy M. Schluchter University of New Orleans, [email protected] Rania Mohamed Mahmoud Joseph Sanfilippo Adam A. Nguyen Johann A. Strnat See next page for additional authors Follow this and additional works at: https://scholarworks.uno.edu/biosciences_facpubs Part of the Microbiology Commons Recommended Citation Mahmoud, R. M., Sanfilippo, J. E., Nguyen, A. A., Strnat, J. A., Partensky, F., Garczarek, L., El Kassem, N. A., Kehoe, D. M., & Schluchter, W. M. (2017). Adaptation to Blue Light in Marine Synechococcus Requires MpeU, an Enzyme with Similarity to Phycoerythrobilin Lyase Isomerases. Frontiers in Microbiology, 8. This Article is brought to you for free and open access by the Department of Biological Sciences at ScholarWorks@UNO. It has been accepted for inclusion in Biological Sciences Faculty Publications by an authorized administrator of ScholarWorks@UNO. For more information, please contact [email protected]. Authors Wendy M. Schluchter, Rania Mohamed Mahmoud, Joseph Sanfilippo, Adam A. Nguyen, Johann A. Strnat, Frédéric Partensky, Laurence Garczarek, Nabil Kassem, and David M. Kehoe This article is available at ScholarWorks@UNO: https://scholarworks.uno.edu/biosciences_facpubs/37 fmicb-08-00243 February 17, 2017 Time: 18:21 # 1 ORIGINAL RESEARCH published: 21 February 2017 doi: 10.3389/fmicb.2017.00243 Adaptation to Blue Light in Marine Synechococcus Requires MpeU, an Enzyme with Similarity to Phycoerythrobilin Lyase Isomerases Rania M. Mahmoud1,2†, Joseph E. Sanfilippo1†, Adam A. Nguyen3,4, Johann A. -
I Topic - Algal Pigments and Algal Classification(ALGAE) Prepared by –Prof.(Dr.)Jainendra Kumar Coordinated By: Prof.(Dr) Shyam Nandan Prasad
Course- M.Sc. Botany Part -I Paper -I Topic - Algal Pigments and algal Classification(ALGAE) Prepared by –Prof.(Dr.)Jainendra Kumar Coordinated by: Prof.(Dr) Shyam Nandan Prasad The algae were broadly divided by F.F.Fritsch (1935) into eleven classes according to their colour - 1. Chlorophyceae or green algae 2. Xanthophyceae or yellow-green algae 3. Chrysophyceae 4. Bacillariophyceae or golden-brown algae 5. Cryptophyceae 6. Dinophyceae 7. Chloromonadineae 8. Eugleninae 9. Phaeophyceae or brown algae 10. Rhodophyceae or red algae, and 11. Myxophyceae or blue-green algae Normally, classification of algae is based on - 1. Nuclear Organization 2. Nature of Cell Wall Components 3. Pigmentation and Photosynthetic Apparatus The pigment is one of the most important criteria used in differentiation of classes in algae. The pigments in algae can be chlorophylls, carotenoids and biloproteins. These pigments are present in sac like structures called thylakoids. The thylakoids are arranged in stacks in the granum of the chloroplasts. Different groups of algae have different types of pigments and organization of thylakoids in chloroplast. The chlorophylls in algae are chlorophyll a, b, c, d and e types. Chlorophyll a is present in all classes of algae. Chlorophyll b is primary pigment of Chlorophyceae and Euglenineae. Chlorophyll c is found in Phaeophyceae and Cryptophyceae. Chlorophyll d is found in Rhodophyceae. Chlorophyll e is confined to Tribonema of Xanthophyceae. Pigments are chemical compounds which reflect only certain wavelengths of visible light. This makes them appear colourful. More important than their reflection of light is the ability of pigments to absorb certain wavelengths. Since each pigment reacts with only a narrow range of the spectrum, it is important for algae to produce pigments of different colours to capture more of the sun's energy. -
Coexistence of Phycoerythrin and a Chlorophyll A/B Antenna in a Marine Prokaryote (Prochlorophyta/Cyanobacteria/Phycobilins/Photosynthesis/Endosymbiosis) WOLFGANG R
Proc. Natl. Acad. Sci. USA Vol. 93, pp. 11126-11130, October 1996 Microbiology Coexistence of phycoerythrin and a chlorophyll a/b antenna in a marine prokaryote (Prochlorophyta/cyanobacteria/phycobilins/photosynthesis/endosymbiosis) WOLFGANG R. HESs*t, FREDEIRIC PARTENSKYt, GEORG W. M. VAN DER STAAYI, JOSE' M. GARCIA-FERNANDEZt, THOMAS BORNER*, AND DANIEL VAULOTt *Department of Biology, Humboldt-University, Chausseestrasse 117, D-10115 Berlin, Germany; and tStation Biologique de Roscoff, Centre National de la Recherche Scientifique Unite Propre de Recherche 9042 and Universite Pierre et Marie Curie, BP 74, F-29682 Roscoff Cedex, France Communicated by Hewson Swift, The University of Chicago, Chicago, IL, July 1Z 1996 (received for review June 7, 1996) ABSTRACT Prochlorococcus marinus CCMP 1375, a ubiq- tation maximum of the major chromophore bound by PE-III uitous and ecologically important marine prochlorophyte, corresponds to that of phycourobilin. was found to possess functional genes coding for the a and 1 subunits of a phycobiliprotein. The latter is similar to phy- coerythrins (PE) from marine Synechococcus cyanobacteria MATERIALS AND METHODS and bind a phycourobilin-like pigment as the major chro- Flow Cytometric Measurements. Sea water samples were mophore. However, differences in the sequences of the ca and collected at different depths during the France-Joint Global 13 chains compared with known PE subunits and the presence Ocean Flux Study OLIPAC cruise held in November 1994 of a single bilin attachment site on the a subunit designate it aboard the N.O. l'Atalante. Samples were analyzed immedi- as a novel PE type, which we propose naming PE-III. P. ately using a FACScan (Becton Dickinson) flow cytometer and marinus is the sole prokaryotic organism known so far that cell concentrations of Prochlorococcus and Synechococcus contains chlorophylls a and b as well as phycobilins. -
Marine Algae and Land Plants Share Conserved Phytochrome Signaling Systems
Marine algae and land plants share conserved phytochrome signaling systems Deqiang Duanmua,1, Charles Bachyb,1, Sebastian Sudekb, Chee-Hong Wongc, Valeria Jiménezb, Nathan C. Rockwella, Shelley S. Martina, Chew Yee Nganc, Emily N. Reistetterb, Marijke J. van Barenb, Dana C. Priced, Chia-Lin Weic, Adrian Reyes-Prietoe,f, J. Clark Lagariasa,2, and Alexandra Z. Wordenb,f,2 aDepartment of Molecular and Cellular Biology, University of California, Davis, CA 95616; bMonterey Bay Aquarium Research Institute, Moss Landing, CA 95039; cSequencing Technology Group, Joint Genome Institute, Lawrence Berkeley National Laboratory, Walnut Creek, CA 94598; dDepartment of Ecology, Evolution, and Natural Resources, Institute of Marine and Coastal Sciences, Rutgers University, New Brunswick, NJ 08903; eBiology Department, University of New Brunswick, Fredericton, NB, Canada E3B5A3; and fIntegrated Microbial Biodiversity Program, Canadian Institute for Advanced Research, Toronto, ON, Canada M5G 1Z8 Contributed by J. Clark Lagarias, September 3, 2014 (sent for review June 18, 2014) Phytochrome photosensors control a vast gene network in duce light signals into biochemical outputs that shape overall streptophyte plants, acting as master regulators of diverse growth organismal responses (1, 13). and developmental processes throughout the life cycle. In contrast Although plant phytochromes control vast, complicated gene with their absence in known chlorophyte algal genomes and most networks, their origin, evolution, and ancestral signaling mech- sequenced prasinophyte -
BOT*4380, Course Outline, Winter 2016
University of Guelph College of Biological Science Department of Molecular and Cellular Biology COURSE OUTLINE Metabolism in the Whole Life of Plants-BOT 4380 Winter 2016 Course Description This course follows the developmental changes that take place in plants, and explores the molecular, biochemical, and physiological mechanisms that are responsible for development. Emphasis will be placed on the importance of modern experimental methods and critical evaluation of the data. 0.5 U. Prerequisites: BIOL*1040 or BIOL*1090 & BIOC 2580. Teaching Team Dr. Tariq Akhtar, Science Complex, Room 4461, Ext. 54794, [email protected] & Dr. Barry Micallef, CRSC Rm 424, Ext. 54384, [email protected]. Office hours are flexible, and we will be available for discussion after class or by appointment. Feel free to contact us by email; we will do our best to respond quickly. Course Schedule Lectures are in MCKN (MacKinnon) 116, 10:30-11:20 am, Mon/Wed/Fri, starting Monday, January 11th, 2016 and ending Friday, April 8th, 2016 (35 lectures total). Learning Goals and Rationale By the end of this course, students should be able to: 1. grasp both the historical development and the current state of knowledge in plant biology, and in plant metabolism in particular, including an appreciation of emerging technologies and experimental methods; 2. integrate the physiological, biochemical, and molecular mechanisms whereby autotrophic organisms, and particularly seed plants, sustain themselves in the context of the whole life cycle of the plant; 3. interpret the scientific literature and data relevant to plant biology and to plant metabolism in particular; 4. communicate effectively using scientific writing; 5. -
The Roles of the Chaperone-Like Protein Cpez and the Phycoerythrobilin Lyase Cpey in Phycoerythrin Biogenesis
University of New Orleans ScholarWorks@UNO Biological Sciences Faculty Publications Department of Biological Sciences 2019 The Roles of the Chaperone-like Protein CpeZ and the Phycoerythrobilin Lyase CpeY in Phycoerythrin Biogenesis Wendy M. Schluchter University of New Orleans, [email protected] D. M. Kehoe J. A. Karty T. Blensdorf A. Gutu See next page for additional authors Follow this and additional works at: https://scholarworks.uno.edu/biosciences_facpubs Part of the Biology Commons Recommended Citation Kronfel, C. M., Biswas, A., Frick, J. P., Gutu, A., Blensdorf, T., Karty, J. A., Kehoe, D. M., & Schluchter, W. M. (2019). The roles of the chaperone-like protein CpeZ and the phycoerythrobilin lyase CpeY in phycoerythrin biogenesis. Biochimica et Biophysica Acta, 1860(7), 549–561. (post print) This Article Post-Print is brought to you for free and open access by the Department of Biological Sciences at ScholarWorks@UNO. It has been accepted for inclusion in Biological Sciences Faculty Publications by an authorized administrator of ScholarWorks@UNO. For more information, please contact [email protected]. Authors Wendy M. Schluchter, D. M. Kehoe, J. A. Karty, T. Blensdorf, A. Gutu, J. P. Frick, A. Biswas, and C. M. Kronfel This article post-print is available at ScholarWorks@UNO: https://scholarworks.uno.edu/biosciences_facpubs/42 The roles of the chaperone-like protein CpeZ and the phycoerythrobilin lyase CpeY in phycoerythrin biogenesis Christina M. Kronfela1, Avijit Biswasb2, Jacob P. Fricka, Andrian Gutuc3, Tyler Blensdorfd4, Jonathan A. Kartyd, David M. Kehoec, Wendy M. Schluchtera* From the aDepartments of Biological Sciences and bChemistry, University of New Orleans, New Orleans, LA 70148, USA; cDepartment of Biology, Indiana University, Bloomington, IN 47405, USA; dDepartment of Chemistry, Indiana University, Bloomington, IN 47405, USA *To whom the correspondence should be addressed: Dr. -
Two Classes of Pigments, Carotenoids and C-Phycocyanin, in Spirulina Powder and Their Antioxidant Activities
molecules Article Two Classes of Pigments, Carotenoids and C-Phycocyanin, in Spirulina Powder and Their Antioxidant Activities Woo Sung Park 1,†, Hye-Jin Kim 1,†, Min Li 2, Dong Hoon Lim 3, Jungmin Kim 4, Sang-Soo Kwak 5, Chang-Min Kang 4, Mario G. Ferruzzi 2,* and Mi-Jeong Ahn 1,* ID 1 College of Pharmacy and Research Institute of Pharmaceutical Sciences, Gyeongsang National University, Jinju 52828, Korea; [email protected] (W.S.P.); [email protected] (H.-J.K.) 2 Plants for Human Health Institute, North Carolina State University, Kannapolis, NC 28081, USA; [email protected] 3 Department of Information and Statistics and RINS, Gyeongsang National University, Jinju 52828, Korea; [email protected] 4 Korea Institute of Toxicology, Jinju 52834, Korea; [email protected] (J.K.); [email protected] (C.-M.K.) 5 Plant Systems Engineering Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Korea; [email protected] * Correspondence: [email protected] (M.G.F.); [email protected] (M.-J.A.); Tel.: +82-55-772-2425 (M.-J.A.) † Both first authors contributed equally to this work. Received: 24 July 2018; Accepted: 15 August 2018; Published: 17 August 2018 Abstract: Arthrospira platensis is the widely available source of spirulina that contains distinctive natural pigments, including carotenoids and C-phycocyanin (C-PC). In this study, the major carotenoid and C-PC contents were determined in seven commercially available spirulina powder products and laboratory-prepared A. platensis trichomes (AP-1) by an LC-DAD method and UV-Visible spectrometry, respectively. The correlation of these two pigment content levels with Hunter color coordinates and antioxidant activity was also evaluated.