Chlorophyllide a Reductase Cat

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chlorophyllide a reductase Cat. No. EXWM-1396 Lot. No. (See product label) Introduction Description The enzyme, together with EC 1.1.1.396, bacteriochlorophyllide-a dehydrogenase, and EC 4.2.1.165, chlorophyllide-a 31-hydratase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. These enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. This enzyme catalyses a trans-reduction of the B-ring; the product has the (7R,8R)-configuration. In addition, the enzyme has a latent activity of EC 1.3.7.13, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin). The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction. Synonyms bchX (gene name); bchY (gene name); bchZ (gene name); COR Product Information Form Liquid or lyophilized powder EC Number EC 1.3.7.15 Reaction (1) 3-deacetyl-3-vinylbacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+; (2) bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+; (3) 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+ Notes This item requires custom production and lead time is between 5-9 weeks. We can custom produce according to your specifications. Storage and Shipping Information Creative Enzymes. All rights reserved. 45-1 Ramsey Road, Shirley, NY 11967, USA Tel:1-631-562-8517 1-516-512-3133 Fax:1-631-938-8127 E-mail: [email protected] http://www.creative-enzymes.com Storage Store it at +4 ℃ for short term. For long term storage, store it at -20 ℃~-80 ℃. Creative Enzymes. All rights reserved. 45-1 Ramsey Road, Shirley, NY 11967, USA Tel:1-631-562-8517 1-516-512-3133 Fax:1-631-938-8127 E-mail: [email protected] http://www.creative-enzymes.com.

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1 Introduction
Introduction 1 1 Introduction Tetrapyrroles belong to a group of molecules with a common structure. They are synthesized in a branched pathway, in which various end products are formed to different amounts. The most abundant cyclic tetrapyrroles are chlorophyll (Chl) and heme, which are characterized by a chelated magnesium and ferrous ion, respectively. Chlorophyll is involved in light absorption and energy transduction during photosynthesis. Heme is a cofactor of hemoglobin, cytochromes, P450 mixed-function oxygenases, and catalases. Other members of the class of tetrapyrroles include siroheme (the prosthetic group of nitrite and sulphite reductases) and phytochromobilin, the chromophore of phytochrome, which is involved in light perception. Tetrapyrrole biosynthesis has been the subject of numerous studies over several decades. But genetic and biochemical characterization of tetrapyrrole biosynthesis has progressed by using approaches to genetically dissect the tetrapyrrole biosynthetic pathway. Pigment-deficient mutants and antisense technology have proved to be useful for examining the mechanisms of metabolic control or for analyzing biochemically the enzymatic steps which are affected by the mutation or by the antisense RNA expression. Tetrapyrrole intermediates are highly photoreactive. They can easily be excited and transfer the energy or electrons to O2. Then reactive oxygen species (ROS) are produced upon exposure to light and oxygen. Under normal growth conditions the risk of photooxidative damage from intermediates in tetrapyrrole biosynthesis is low. Excessive accumulation of such intermediates is the result of deregulation of tetrapyrrole biosynthesis. Toxic effects of porphyrins are evident in human patients with deficiencies of one of the enzymes of heme biosynthesis. These patients are suffering from metabolic diseases, which are called porphyrias (Moore, 1993).
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TION of BUCKWHEAT. It Has Been Known for a Long Time That Certain
PHOTOSENSITIZATION OF ANIMALS AFTER THE INGES- TION OF BUCKWHEAT. BY CHARLES SHEARD, PH.D., HAROLD D. CAYLOR, M.D., AND CARL SCHLOTTHAUER, D.V.M. (From tke Section on Pkysics and Biophysical Research, tke Section on Surgical Pathology, and the Division of Experimental Palhdogy and Surgery, Mayo Clinic and The Mayo Foundation, Rochester, Minnesota.) (Received for publication,~'March 1, 1928.) It has been known for a long time that certain animals, following the ingestion of various substances, are rendered sensitive to certain types of radiant energy. The present study covers biologic and physical observations on the degree of sensitization, the character of the sensitizing light and the nature of the photodynamic substance of buckwheat. White rabbits, mice, rats, goats, swine, dogs and varicolored guinea pigs were studied. Sunlight, carbon arc lamp (Efka or Hoffman) with Conradty-Norris vacuum carbon electrodes and quartz mercury vapor arcs (Victor X-Ray Corporation), both with and without various filters, were employed for irradiation. All of these sources contain infra-red, visible and ultra-violet radiations. I~SLr~ OF LITERATURE. Considerable literature, especially European, has appeared on the subject of diseases in animals and man brought about by optical sensitization. Somewhat detailed accounts of the contributions relative to diseases due to exogenous sensi- tization are to be found in the brochures by Hausmann and by Mayer. Years ago European stockmen found that in certain animals which had ingested buckwheat (plant or seed), erythema, itching, edema and convulsions developed and, in many cases, paralysis and death, on exposure to out-of-door sunshine. However, untoward symptoms did not arise if the animals were kept indoors or in partial darkness and they recovered from the sensitization induced by eating certain plants if they were removed from the light early in the onset of the symp- toms.
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Chlorophyll Biosynthesis
Chlorophyll Biosynthesis: Various Chlorophyllides as Exogenous Substrates for Chlorophyll Synthetase Jürgen Benz and Wolfhart Rüdiger Botanisches Institut, Universität München, Menziger Str. 67, D-8000 München 19 Z. Naturforsch. 36 c, 51 -5 7 (1981); received October 10, 1980 Dedicated to Professor Dr. H. Merxmüller on the Occasion of His 60th Birthday Chlorophyllides a and b, Protochlorophyllide, Bacteriochlorophyllide a, 3-Acetyl-3-devinylchlo- rophyllide a, Pyrochlorophyllide a, Pheophorbide a The esterification of various chlorophyllides with geranylgeranyl diphosphate was investigated as catalyzed by the enzyme chlorophyll synthetase. The enzyme source was an etioplast membrane fraction from etiolated oat seedlings ( Avena sativa L.). The following chlorophyllides were prepared from the corresponding chlorophylls by the chlorophyllase reaction: chlorophyllide a (2) and b (4), bacteriochlorophyllide a (5), 3-acetyl-3-devinylchlorophyllide a (6), and pyro chlorophyllide a (7). The substrates were solubilized with cholate which reproducibly reduced the activity of chlorophyll synthetase by 40-50%. It was found that the following compounds were good substrates for chlorophyll synthetase: chlorophyllide a and b, 3-acetyl-3-devinylchloro- phyllide a, and pyrochlorophyllide a. Only a poor or no reaction was found with protochloro phyllide, pheophorbide a, and bacteriochlorophyllide. This difference of reactivity was not due to distribution differences of the substrates between solution and pelletable membrane fraction. Furthermore, no interference between good and poor substrate was detected. Structural features necessary for chlorophyll synthetase substrates were discussed. Introduction Therefore no exogenous 2 was applied. The only substrate was 2 formed by photoconversion of endo The last steps of chlorophyll a (Chi a) biosynthe genous Protochlide (1) in the etioplast membrane.
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Surprising Roles for Bilins in a Green Alga Jean-David Rochaix1 Departments of Molecular Biology and Plant Biology, University of Geneva,1211 Geneva, Switzerland
COMMENTARY COMMENTARY Surprising roles for bilins in a green alga Jean-David Rochaix1 Departments of Molecular Biology and Plant Biology, University of Geneva,1211 Geneva, Switzerland It is well established that the origin of plastids which serves as chromophore of phyto- can be traced to an endosymbiotic event in chromes (Fig. 1). An intriguing feature of which a free-living photosynthetic prokaryote all sequenced chlorophyte genomes is that, invaded a eukaryotic cell more than 1 billion although they lack phytochromes, their years ago. Most genes from the intruder genomes encode two HMOXs, HMOX1 were gradually transferred to the host nu- andHMOX2,andPCYA.InPNAS,Duanmu cleus whereas a small number of these genes et al. (6) investigate the role of these genes in were maintained in the plastid and gave the green alga Chlamydomonas reinhardtii rise to the plastid genome with its associated and made unexpected ﬁndings. protein synthesizing system. The products of Duanmu et al. ﬁrst show that HMOX1, many of the genes transferred to the nucleus HMOX2, and PCYA are catalytically active were then retargeted to the plastid to keep it and produce bilins in vitro (6). They also functional. Altogether, approximately 3,000 demonstrate in a very elegant way that these nuclear genes in plants and algae encode proteins are functional in vivo by expressing plastid proteins, whereas chloroplast ge- a cyanobacteriochrome in the chloroplast Fig. 1. Tetrapyrrole biosynthetic pathways. The heme nomes contain between 100 and 120 genes of C. reinhardtii, where, remarkably, the and chlorophyll biosynthetic pathways diverge at pro- (1). A major challenge for eukaryotic pho- photoreceptor is assembled with bound toporphyrin IX (ProtoIX).
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Spatial and Temporal Variability in the Response of Phytoplankton and Bacterioplankton to B-Vitamin Amendments in an Upwelling S
1 Spatial and temporal variability in the response of 2 phytoplankton and bacterioplankton to B-vitamin 3 amendments in an upwelling system 4 Vanessa Joglar1*, Antero Prieto1, Esther Barber-Lluch1, Marta Hernández-Ruíz1, Emilio 5 Fernández1 and Eva Teira1 6 1 Centro de Investigación Mariña da Universidade de Vigo (CIM-UVigo), Departamento Ecoloxía e 7 Bioloxía Animal, Universidade de Vigo, Campus Lagoas-Marcosende, Vigo, 36310, Spain 8 *Correspondence to: Vanessa Joglar +34 986 818790 ([email protected]) 9 1 10 Abstract. We experimentally evaluated the temporal (inter-day and inter-season) and 11 spatial variability in microbial plankton responses to vitamin B12 and/or B1 supply 12 (solely or in combination with inorganic nutrients) in coastal and oceanic waters of the 13 northeast Atlantic Ocean. Phytoplankton and, to a lesser extent, prokaryotes were strongly 14 limited by inorganic nutrients. Inter-day variability in microbial plankton responses to B- 15 vitamins was limited compared to inter-season variability, suggesting that B-vitamins 16 availability might be partially controlled by factors operating at seasonal scale. 17 Chlorophyll-a (Chl-a) concentration and prokaryote biomass (PB) significantly increased 18 after B-vitamin amendments in 13 % and 21 %, respectively, of the 216 cases (36 19 experiments × 6 treatments). Most of these positive responses were produced by 20 treatments containing either B12 solely or B12 combined with B1 in oceanic waters, 21 which was consistent with the significantly lower average vitamin B12 ambient 22 concentrations compared to that in the coastal station. Negative responses, implying a 23 decrease in Chl-a or PB, represented 21 % for phytoplankton and 26 % for prokaryotes.
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Catabolism of Tetrapyrroles As the Final Product of Heme Catabolism (Cf Scheme 1)
CHEMIE IN FREIBURG/CHIMIE A FRIBOURG 352 CHIMIA 48 (199~) Nr. 9 (Scl'lcmhcr) ns itu Chimia 48 (/994) 352-36/ heme (1), at the a-methene bridge (C(5)) €> Neue Sclnveizerische Chemische Gesellschaft producing CO and an unstable Felli com- /SSN 0009-4293 plex. The latter loses the metal ion to yield the green pigment protobiliverdin IXa (usually abbreviated to biliverdin (2)), which is excreted by birds and amphibia, Catabolism of Tetrapyrroles as the final product of heme catabolism (cf Scheme 1). The iron is recovered in the protein called ferritin and can be reutilized Albert Gossauer* for the biosynthesis of new heme mole- cules. As biliverdin (2) has been recog- nized to be a precursor in the biosynthesis of phycobilins [9], a similar pathway is Abstract. The enzymatic degradation of naturally occurring tetrapyrrolic pigments probably followed for the biosynthesis of (heme, chlorophylls, and vitamin B 12) is shortly reviewed. this class oflight-harvesting chromophores 1. Introduction pounds known so far are synthesized, have Scheme I. Catabolism (!{ Heme ill Mammals been already elucidated, it may be antici- In contrast to the enormous amount of pated that the study of catabolic processes work accomplished by chemists in the will attract the interest of more chemists elucidation of biosynthetic pathways of and biochemists in the near future. secondary metabolites (terpenes, steroids, alkaloids, among others), only a few at- tempts have been made until now to un- 2. Heme Catabolism derstand the mechanisms oftheirdegrada- tion in living organisms. A possible rea- It has been known for over half a cen- son for this fact is the irrational association tury that heme, the oxygen-carrier mole- of degradation (catabolism: greek Kara= cule associated with the blood pigment down) with decay and, thus, with unattrac- hemoglobin, is converted in animal cells tive dirty colors and unpleasant odors.
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Continuous Chlorophyll Degradation Accompanied by Chlorophyllide and Phytol Reutilization for Chlorophyll Synthesis in Synechocystis Sp
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Biochimica et Biophysica Acta 1767 (2007) 920–929 www.elsevier.com/locate/bbabio Continuous chlorophyll degradation accompanied by chlorophyllide and phytol reutilization for chlorophyll synthesis in Synechocystis sp. PCC 6803 ⁎ Dmitrii Vavilin, Wim Vermaas School of Life Sciences and Center for the Study of Early Events in Photosynthesis, Arizona State University, Box 874501, Tempe, AZ 85287, USA Received 3 January 2007; received in revised form 23 March 2007; accepted 27 March 2007 Available online 3 April 2007 Abstract Chlorophyll synthesis and degradation were analyzed in the cyanobacterium Synechocystis sp. PCC 6803 by incubating cells in the presence of 13C-labeled glucose or 15N-containing salts. Upon mass spectral analysis of chlorophyll isolated from cells grown in the presence of 13C-glucose for different time periods, four chlorophyll pools were detected that differed markedly in the amount of 13C incorporated into the porphyrin (Por) and phytol (Phy) moieties of the molecule. These four pools represent (i) unlabeled chlorophyll (12Por12Phy), (ii) 13C-labeled chlorophyll (13Por13Phy), and (iii, iv) chlorophyll, in which either the porphyrin or the phytol moiety was 13C-labeled, whereas the other constituent of the molecule remained unlabeled (13Por12Phy and 12Por13Phy). The kinetics of 12Por12Phy disappearance, presumably due to chlorophyll de- esterification, and of 13Por12Phy, 12Por13Phy, and 13Por13Phy accumulation due to chlorophyll synthesis provided evidence for continuous chlorophyll turnover in Synechocystis cells. The loss of 12Por12Phy was three-fold faster in a photosystem I-less strain than in a photosystem II- less strain and was accelerated in wild-type cells upon exposure to strong light.
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The Function of PROTOPORPHYRINOGEN IX OXIDASE in Chlorophyll Biosynthesis Requires Oxidised Plastoquinone in Chlamydomonas Reinh
The function of PROTOPORPHYRINOGEN IX OXIDASE in chlorophyll biosynthesis requires oxidised plastoquinone in Chlamydomonas reinhardtii Pawel Brzezowski, Brigitte Ksas, Michel Havaux, Bernhard Grimm, Marie Chazaux, Gilles Peltier, Xenie Johnson, Jean Alric To cite this version: Pawel Brzezowski, Brigitte Ksas, Michel Havaux, Bernhard Grimm, Marie Chazaux, et al.. The function of PROTOPORPHYRINOGEN IX OXIDASE in chlorophyll biosynthesis requires oxidised plastoquinone in Chlamydomonas reinhardtii. Communications Biology, Nature Publishing Group, 2019, 2, pp.159. 10.1038/s42003-019-0395-5. cea-02149191 HAL Id: cea-02149191 https://hal-cea.archives-ouvertes.fr/cea-02149191 Submitted on 6 Jun 2019 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution| 4.0 International License ARTICLE https://doi.org/10.1038/s42003-019-0395-5 OPEN The function of PROTOPORPHYRINOGEN IX OXIDASE in chlorophyll biosynthesis requires oxidised plastoquinone in Chlamydomonas reinhardtii 1234567890():,; Pawel Brzezowski 1,2, Brigitte Ksas3, Michel Havaux3, Bernhard Grimm2, Marie Chazaux1, Gilles Peltier1, Xenie Johnson 1 & Jean Alric 1 In the last common enzymatic step of tetrapyrrole biosynthesis, prior to the branching point leading to the biosynthesis of heme and chlorophyll, protoporphyrinogen IX (Protogen) is oxidised to protoporphyrin IX (Proto) by protoporphyrinogen IX oxidase (PPX).
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M Sucrose Solution in Water
Lawrence Berkeley National Laboratory Recent Work Title CIRCULAR DICHROISM STUDIES ON THE STRUCTURE AND THE PHOTOCHEMISTRY OF PROTOCHLOROPHYLLIDE AND CHLOROPHYLLIDE HOLOCHROME Permalink https://escholarship.org/uc/item/3sj8q1hp Author Mathis, Paul Publication Date 1972 eScholarship.org Powered by the California Digital Library University of California Suwuitted to BiochiITlica et LBL-S81 RECElVfiibphysica Acta Preprint lAWRENCE C. IADIAllON' LA ~O~ &,TORY f rEB -l 1972 \ L.lBRARY A ........ l ri,.~UMENTS SEeTln CIRCULAR DICHROISM STUDIES ON THE STRUCTURE AND THE PHOTOCHEMISTRY OF PROTOCHLOROPHYLLIDE AND CHLOROPHYLLIDE HOLOCHROME Paul Mathis and Kenneth Sauer January 1972 AEC Contract No. W -740S-eng-48 For Reference Not to be taken from this room . .. DISCLAIMER This document was prepared as an account of work sponsored by the United States Government. While this document is believed to contain correct information, neither the United States Government nor any agency thereof, nor the Regents bf the University of California, nor any of their employees, makes any warranty, express or implied, or assumes any legal responsibility for the accuracy, completeness, or usefulness of any information, apparatus, product, or process disclosed, or represents that its use would not infringe privately owned rights. Reference herein to any specific commercial product, process, or service by its trade name, trademark, manufacturer, or otherwise, does not necessarily constitute or imply its endorsement, recommendation, or favoring by the United States Government or any agency thereof, or the Regents of the University of California. The views and opinions of authors expressed herein do not necessarily state or reflect those of the United States Government or any agency thereof or the Regents of the University of California.
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And Formation
J Med Genet: first published as 10.1136/jmg.17.1.1 on 1 February 1980. Downloaded from Review article Journal of Medical Genetics, 1980, 17, 1-14 Haems and chlorophylls: comparison of function and formation G A F HENDRY AND 0 T G JONES From the Department ofBiochemistry, The Medical School, University ofBristol, Bristol BS8 ITD In 1844 Verdeill reported that acid treatment of at the same time by McMunn3 of cytochromes, chlorophyll or haem yielded apparently similar red another group of haem proteins. compounds; he even postulated that chlorophylls It was the demonstration by Nencki and co- would contain iron. Hoppe-Seyler2 confirmed the workers 45 that the degradation of both chlorophylls apparent similarity of acid derivatives of haems and and haems yielded monopyrroles that led them, in chlorophylls from their light absorption charac- true neo-Darwinian fashion, to postulate a common teristics, a point rather overshadowing the discovery origin for animals and plants. 0 0-'I CH2 II copyright. CH CH3 COOH CIH2 CH2 C-O CH2 http://jmg.bmj.com/ NH2 ( CH3' 'CH3 ® 5- Aminolaevulinic acid a CH2 2 1 12 2 CH2 )H COOH CD FIG 1 Structures ofprotohaem and Protoporphyrin IX chlorophyll a and two of their precursors, acid and 5-aminolaevulinic on September 30, 2021 by guest. Protected protoporphyrin IX (with substituent numbering positions). CH2 CH CH.--,j CH2 CH2 COOCH3 Protohoem (haem- b) CooC20H39 Chlorophyll a 1 J Med Genet: first published as 10.1136/jmg.17.1.1 on 1 February 1980. Downloaded from 2 G A F Hendry and 0 T G Jones Following the work ofWillstatter6 and Fischer and particularly those of avian egg shells, have no Stern,7 the structure of most natural and many central complexed metal.
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Biosynthesis of Food Constituents: Natural Pigments. Part 1 – a Review
Czech J. Food Sci. Vol. 25, No. 6: 291–315 Biosynthesis of Food Constituents: Natural Pigments. Part 1 – a Review Jan VELÍŠEK, Jiří DAVÍDEK and Karel CEJPEK Department of Food Chemistry and Analysis, Faculty of Food and Biochemical Technology, Institute of Chemical Technology in Prague, Prague, Czech Republic Abstract VELÍŠEK J., DAVÍDEK J., CEJPEK K. (2007): Biosynthesis of food constituents: Natural pigments. Part 1 – a re- view. Czech J. Food Sci., 25: 291–315. This review article gives a survey of the generally accepted biosynthetic pathways that lead to the most important natural pigments in organisms closely related to foods and feeds. The biosynthetic pathways leading to hemes, chlo- rophylls, melanins, betalains, and quinones are described using the enzymes involved and the reaction schemes with detailed mechanisms. Keywords: biosynthesis; tetrapyrroles; hemes; chlorophylls; eumelanins; pheomelanins; allomelanins; betalains; betax- anthins; betacyanins; benzoquinones; naphthoquinones; anthraquinones Natural pigments are coloured substances syn- noids. Despite their varied structures, all of them thesised, accumulated in or excreted from living are synthesised by only a few biochemical path- or dying cells. The pigments occurring in food ways. There are also groups of pigments that defy materials become part of food, some other pig- simple classification and pigments that are rare ments have been widely used in the preparation or limited in occurrence. of foods and beverages as colorants for centuries. Many foods also owe their colours to pigments that 1 TETRAPYRROLES form in food materials and foods during storage and processing as a result of reactions between food Tetrapyrroles (tetrapyrrole pigments) represent a constituents, notably the non-enzymatic browning relatively small group of pigments that contribute reaction and the Maillard reaction.
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Growth of Haematococcus Pluvialis Flotow in Alternative Media L
http://dx.doi.org/10.1590/1519-6984.23013 Original Article Growth of Haematococcus pluvialis Flotow in alternative media L. H. Sipaúba-Tavaresa*, F. A. Berchielli-Moraisa and B. Scardoeli-Truzzia aLimnology and Plankton Production Laboratory, Aquaculture Center, Universidade Estadual Paulista “Júlio de Mesquita Filho” – UNESP, Via de Acesso Prof. Paulo D. Castellane, s/n, CEP 14884-900, Jaboticabal, SP, Brazil *e-mail: [email protected] Received: December 10, 2013 – Accepted: May 22, 2014 – Distributed: November 30, 2015 (With 3 figures) Abstract Current study investigates the effect of two alternative media: NPK (20-5-20) fertilizer and NPK plus macrophyte (M+NPK) compared to the commercial medium (WC) under growth rate and physiological parameters in batch culture mode (2-L), and verifies whether the use of fertilizer (NPK) and macrophyte (Eichhornia crassipes) would be a good tool for Haematococcus pluvialis culture in the laboratory. The highest number of cells of H. pluvialis has been reported in NPK medium (5.4 × 105cells.mL–1) on the 28th day, and in the M+NPK and WC media (4.1 × 105 cells.mL–1 and 2.1 × 105 cells.mL–1) on the 26th day, respectively. Chlorophyll-a contents were significantly higher (p<0.05) in NPK medium (41-102 µg.L–1) and lower in WC and M+NPK media (14-61 µg.L–1). The astaxanthin content was less than 0.04 mg.L–1. Production cost of 10-L of H. pluvialis was low in all media, and NPK and M+NPK media had a cost reduction of 65% and 82%, respectively when compared with commercial medium (WC).
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