Postharvest Biology and Technology of Fruits, Vegetables, and Flowers

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BIOSENSOR-BASED TECHNOLOGIES 425 Linker layer Gold layer Glass layer CM5 sensor chip Inhibition assay Competition assay Antibody Analyte Immobilized analyte Conjugated analyte Fig. 20.4 Formats for inhibition and competition assays. Inhibition: Free analyte inhibits binding of the antibody to the immobilized analyte on the chip. The signal generated when the antibody binds to the immobilized analyte is inversely proportional to the concentration of free analyte in the sample. Competition: Free ( ) and conjugated ( ) analyte compete for binding to the immobilized antibody. The signal generated is inversely proportional to the amount of free analyte in the sample. between the immobilized and free antigen for antibody binding. A change in signal is recorded, and this is inversely proportional to the amount of target molecule that remains free in solution. An alternative method to detect analytes of interest involves a competitive assay. In this format, the antibody is immobilized on the surface of a suitable matrix, and the sample is mixed with a standard target molecule that has been conjugated to a large carrier protein. This results in the sample and the conjugated standard competing for the immobilized antibody on the surface of the biochip. An increase in signal is caused by the binding of the large analyte–carrier conjugate, and the data generated is similar to the inhibition assay since the signal recorded is inversely proportional to the amount of target molecule present in the sample. 20.3.1 Immunobiosensors Many biosensor-based assays have utilized antibodies (immunoglobulins) as the molecular recognition element, leading to the adoption of the term “immunobiosensor.” Antibodies are the key recognition elements of the immune system, and various antibodies and antibodyderived fragments have been produced with the capability of detecting a remarkable variety of diverse analytes (Dillon et al., 2005). Antibodies are globular glycoproteins (sugarcontaining proteins), with five classes (or serotypes) existing—IgA, IgM, IgE, IgD, and IgG. Single antibody molecules typically have molecular weights of ∼150–200 Da. IgG
426 POSTHARVEST BIOLOGY & TECHNOLOGY OF FRUITS, VEGETABLES, & FLOWERS Complementarity determining regions Heavy chain Light chain V H Intrachain disulphide bond C H1 V L C L Hinge region Carbohydrate C H2 Interchain disulphide bond C H3 Fig. 20.5 A general schematic diagram of an IgG antibody. The following terms are used in the diagram: V H , variable heavy region; V L , variable light region; C H , constant heavy region; C L , constant light region. The location of the carbohydrate moiety attached to the C H2 constant region is also shown. antibodies (Fig. 20.5) have a Y-shaped backbone with four polypeptide chains located in two identical chains that are covalently attached through disulfide bonds. The innermost chains are referred to as the heavy chains because they are approximately double the molecular weight of the outer arms (termed the light chains). The recognition sites of the antibody (which interact with an epitope on an antigen) are located at the ends of the V H (variable heavy) and V L (variable light) regions of the heavy and light chains. They are commonly referred to as the complementarity-determining regions (CDRs). Each arm of an antibody can bind to one antigen, so one IgG molecule can theoretically bind to two antigens. The strength of an antibody–antigen interaction is referred as the “affinity” of the antibody. This is important when using an antibody in an immunosensor-based system to detect the presence or absence of an antigen in a fruit or vegetable sample. There are three main methods for generating antibodies that may be implemented in biosensor-based platforms. The production of polyclonal antibodies involves the immunization of animal hosts to generate an immune response toward a particular antigen. Blood samples are subsequently collected, and the antibodies generated are purified from the serum of the animal. These typically consist of a variety of different serotypes with varying affinities/specificities toward the epitope in question. Any large animal, including guinea pigs, rabbits, goats, sheep, and donkeys, is capable of producing these antibodies (Leenaars and Hendriksen, 2005). The second method of generating antibodies is by using hybridoma technology to produce monoclonal antibodies (Köhler and Milstein, 1975; Nelson et al., 2000; Hudson and
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Postharvest Biology and Technology
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Edition first published 2008 c○ 2
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vi CONTENTS 9 Structural Deteriorat
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Contributors Ishan Adyanthaya Depar
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x CONTRIBUTORS Gopinadhan Paliyath
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xii PREFACE difficult to find a boo
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Chapter 1 Postharvest Biology and T
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POSTHARVEST BIOLOGY AND TECHNOLOGY
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COMMON FRUITS, VEGETABLES, FLOWERS,
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Chapter 3 Biochemistry of Fruits Go
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BIOCHEMISTRY OF FRUITS 21 et al., 2
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BIOCHEMISTRY OF FRUITS 23 3.2.2 Lip
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BIOCHEMISTRY OF FRUITS 25 exposure
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BIOCHEMISTRY OF FRUITS 27 isoform o
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BIOCHEMISTRY OF FRUITS 29 Maltose
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BIOCHEMISTRY OF FRUITS 31 content i
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BIOCHEMISTRY OF FRUITS 33 control.
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BIOCHEMISTRY OF FRUITS 35 range fro
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BIOCHEMISTRY OF FRUITS 37 six (gluc
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BIOCHEMISTRY OF FRUITS 39 Ethylene
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BIOCHEMISTRY OF FRUITS 41 3.3.3 Pro
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BIOCHEMISTRY OF FRUITS 43 component
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Phenylalanine Phenylalanine ammonia
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BIOCHEMISTRY OF FRUITS 47 coloratio
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BIOCHEMISTRY OF FRUITS 49 Fluhr, R.
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Chapter 4 Biochemistry of Flower Se
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BIOCHEMISTRY OF FLOWER SENESCENCE 5
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PROGRAMMED CELL DEATH DURING PLANT
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(a) (a′) (b) (b′) (c) (d) Fig.
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Chapter 6 Ethylene Perception and G
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ETHYLENE PERCEPTION AND GENE EXPRES
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Chapter 7 Enhancing Postharvest She
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ENHANCING POSTHARVEST SHELF LIFE AN
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THE BREAKDOWN OF CELL WALL COMPONEN
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Table 8.3 Transgenic genetics to de
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Chapter 9 Structural Deterioration
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PHOSPHOLIPASE D, MEMBRANE DETERIORA
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Fig. 9.3 Fracture face of a fully o
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PHOSPHOLIPASE D INHIBITION TECHNOLO
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HEAT TREATMENT FOR ENHANCING POSTHA
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THE ROLE OF POLYPHENOLS 261 mainly
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THE ROLE OF POLYPHENOLS 263 Table 1
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THE ROLE OF POLYPHENOLS 265 Pentose
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THE ROLE OF POLYPHENOLS 267 Phenyla
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THE ROLE OF POLYPHENOLS 269 3' OH H
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THE ROLE OF POLYPHENOLS 271 OH OH O
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THE ROLE OF POLYPHENOLS 273 compoun
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THE ROLE OF POLYPHENOLS 275 washing
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THE ROLE OF POLYPHENOLS 277 (Fujita
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THE ROLE OF POLYPHENOLS 279 Boyer,
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THE ROLE OF POLYPHENOLS 281 Peschel
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ISOPRENOID BIOSYNTHESIS IN FRUITS A
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Chapter 14 Postharvest Treatments A
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POSTHARVEST TREATMENTS AFFECTING SE
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Chapter 15 Polyamines and Regulatio
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POLYAMINES AND REGULATION OF RIPENI
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Chapter 16 Postharvest Enhancement
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POSTHARVEST ENHANCEMENT OF PHENOLIC
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RHIZOSPHERE MICROORGANISMS 361 the
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RHIZOSPHERE MICROORGANISMS 363 Rese
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RHIZOSPHERE MICROORGANISMS 365 Tabl
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RHIZOSPHERE MICROORGANISMS 367 Toma
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RHIZOSPHERE MICROORGANISMS 369 Such
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RHIZOSPHERE MICROORGANISMS 371 Gian
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Chapter 18 Biotechnological Approac
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INDEX 475 LePLDα3 (AY013253), 213-
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INDEX 477 Pectin methylesterase (PM
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INDEX 479 PSY1 expression, 289 PSY1
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INDEX 481 Sugars, biosynthesis of,
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