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METABOLIC ENGINEERING OF THE IODINE CONTENT IN ARABIDOPSIS THALIANA Martina Landini 1 , Silvia Gonzali 1 , Claudia Kiferle 1 , Massimo Tonacchera 2,4 , Patrizia Agretti 2,4 , Antonio Dimida 2,4 , Paolo Vitti 2,4 , Amedeo Alpi 3,4 , Aldo Pinchera 2,4 , Pierdomenico Perata 1 1 PlantLab, Institute of Life Sciences, Scuola Superiore Sant’Anna, Piazza Martiri della Libertà 33, 56127 Pisa, Italy 2 Department of Endocrinology and Metabolism, University of Pisa, Via Paradisa 2, 56124 Pisa, Italy 3 Department of Crop Plant Biology, University of Pisa, Via Mariscoglio 34, 56124 Pisa, Italy 4 Centre of Excellence for the study of damage to the Nervous and Endocrine systems produced by Environmental, Alimentary, and Pharmacological agents, AmbiSEN, University of Pisa Keywords: Arabidopsis, biofortification, iodine, NIS, volatilization Plants are a poor source of iodine, an essential micronutrient for human health. Several attempts of iodine biofortification of crops have been carried out in the recent years, but the scarce knowledge on the physiology of iodine in plants makes results often contradictory and not generalizable. In this work, we used a molecular approach to investigate how the ability of a plant to accumulate iodine can be influenced by different mechanisms. In particular, we demonstrated that the iodine content in Arabidopsis thaliana can be increased either by facilitating its uptake with the overexpression of the human sodium-iodide symporter (NIS) or through the reduction of its volatilization by knockingout HOL-1, a halide methyltransferase. Our experiments show that the iodine content in plants results from a balance between intake and retention and that the increase of the uptake could be useless without a concomitant removal of the volatilization process. A correct manipulation of this mechanism could improve iodine biofortification of crops and prevent the release of the ozone layer-threatening methyl iodide into the atmosphere.
FROM ENZYMATIC BROWNING IN FRUITS AND VEGETABLES TO MODIFICATION OF PROTEINS BY REACTION WITH COPPER, ASCORBATE AND OXYGEN Avi Golan-Goldhirsh Ben-Gurion University of the Negev, Blaustein Institutes for Desert Research French Associates Institute for Agriculture and Biotechnology of Drylands Albert Katz Department of Dryland Biotechnologies Midreshet Ben-Gurion 84990, Israel Keywords: ascorbic acid, copper, enzymatic browning, histidine, polyphenol oxidase Enzymatic browning is common in many fruits and vegetables. The problem is acute especially in food processing. If not taken care off, it may lead to undesirable taste and color and loss of nutritive value. The reaction is catalyzed by polyphenol oxidase, a metallo-enzyme, containing copper as a prosthetic group. Prevention of enzymatic browning by ascorbate is generally thought to involve reduction of the product, a benzoquinone, to O-dihydroxyphenol, the substrate of the enzyme reaction, with the oxidation of ascorbate to dehydroascorbate. However, incubation of polyphenol oxidase with ascorbate alone, without the phenolic substrate, still led to the loss of enzymatic activity, suggesting a non-enzyme catalyzed reaction. It was hypothesized that free copper in solution in the presence of ascorbate catalyzed the reaction. Copper is an essential trace element in most fruits and vegetables. It is necessary for a complete diet. Ascorbate is a vitamin found in most of our plant derived foods. Ascorbate in the presence of added Cu 2+ was effective in inactivation of the enzyme significantly more than either ascorbate, dehydroascorbate or copper, each alone. O 2 was required for the reaction. There were changes in the amino acid composition of polyphenol oxidase following treatment with ascorbate-Cu 2+ . The most distinctive change was a decrease in histidine from 4 to 1 mol/mol enzyme subunit. A similar modification, relatively specific to histidine, was obtained by treatment of other proteins by ascorbate-Cu 2+ . The site-directed specificity toward histidine residues of proteins can best be explained by postulating that the Cu 2+ involved in the reaction is bound to the imidazole group of histidine prior to reaction with ascorbate ion and O 2 . There is indirect evidence that the reactive system leading to degradation of histidine residues in proteins is a quaternary complex between the imidazole group, Cu 2+ , ascorbate and O 2 reacting to form reactive species in proximity to the imidazole group leading to its degradation. The involvement of heavy metals, especially copper, in modification of proteins in food, is it beneficial or damaging?
Page 1: PROCEEDING OF
Page 4 and 5: INTERNATIONAL SCIENTIFIC COMMITTEE:
Page 6 and 7: Second Annual Conference and MC Mee
Page 8 and 9: 16:30 16:30- Zeshan Hassan, Sangita
Page 10 and 11: processes 16:10 Coffee break 16:30
Page 13 and 14: HOW TO INFLUENCE THE CD CONTENT IN
Page 15 and 16: ZN UPTAKE BY WHEAT IN THE PRESENCE
Page 17 and 18: NANOSIMS: A TECHNIQUE FOR SUBCELLUL
Page 19 and 20: IN VITRO MINERAL AVAILABILITY IN PE
Page 21 and 22: RECENT ADVANCES IN COMPARTMENTATION
Page 23 and 24: production, breeding and processing
Page 25 and 26: SUBSTANTIAL NATURAL VARIATION IN MI
Page 27 and 28: ADAPTIVE MECHANISMS OF HYPERACCUMUL
Page 29 and 30: BREEDING CROPS FOR BETTER NUTRITION
Page 31 and 32: Fig 1, 190x showing biochar’s var
Page 33 and 34: V. SIMULTANEOUS BIOFORTIFICATION OF
Page 35: PCP1 AND ATOSA1: PROTEINS INVOLVED
Page 39 and 40: PROGRESS IN THE UNDERSTANDING OF CA
Page 41 and 42: THE ROLE OF BIOCHAR IN THE PHYTOREM
Page 43 and 44: PHYSIOLOGICAL CHARACTERIZATION AND
Page 45: ARSENIC IN RICE: GASTROINTESTINAL B
Page 49 and 50: SALINITY AND MYCORRHIZAL SYMBIOSIS:
Page 51 and 52: ALIMURGIC HERBS AS POTENTIAL SOURCE
Page 53 and 54: EFFECTS OF BIOCHAR AND GREENWASTE C
Page 55 and 56: UPTAKE OF ARSENIC INTO TOMATO PLANT
Page 57 and 58: EFFECTS OF SELENIUM ON THE GROWTH P
Page 59 and 60: EFFECT OF ADDITION OF SULPHUR FERTI
Page 61 and 62: I. SIMULTANEOUS BIOFORTIFICATION OF
Page 63 and 64: EFFECTS OF BIO-(PHYTO-, FUNGI) GENI
Page 65 and 66: ASSESSMENT OF HEAVY METAL (PB, CD,
Page 67 and 68: ZINC FLUXES INTO THE DEVELOPING BAR
Page 69 and 70: THE PRESENCE OF COPPER (Cu 2+ ) IN
Page 71 and 72: DETECTION OF CADMIUM DISTRIBUTION I
Page 73 and 74: DETERMINATION OF POLLUTION OF DRINK
Page 75 and 76: EARLY RESPONSES IN ROOT MERISTEM OF
Page 77 and 78: BUCKWHEAT PRODUCTION ON ACID AND LO
Page 79 and 80: THE IMPACT OF HEAVY METALS ON RED C
Page 81 and 82: HOW TO ENHANCE NUTRIENT ASSIMILATIO
Page 83 and 84: CONTROLLING CADMIUM ACCUMULATION IN
Page 85 and 86: RESPONSES OF SORGHUM PLANTS TO STRE
Page 87 and 88:
TO BE ECO, OR NOT TO BE? - SOME ASP
Page 89 and 90:
III. SIMULTANEOUS BIOFORTIFICATION
Page 91 and 92:
TRACE ELEMENTS, GLUTATHIONE AND DIA
Page 93 and 94:
COMPOST INCORPORATION IN SOIL DECRE
Page 95 and 96:
INFLUENCE OF PUTRESCINE APPLICATION
Page 97 and 98:
POSSIBLE NICOTIANAMINE INVOLVEMENT
Page 99 and 100:
NUTRITIONAL QUALITY OF SELECTED SPR
Page 101:
HOW DOES THE GREEN REVOLUTION AFFEC
Page 105 and 106:
Aarts Mark; Lab. of Genetics, Wagen
Page 107 and 108:
Lacatusu Radu; National Research In
Page 109:
Schwitzguebel Jean-Paul; EPFL, Labo
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