Polyphenol oxidase purification

Chazarra S, Garcia-Carmona F and Cabanes, J. 2001. Evidence for a tetrameric form of iceberg lettuce (Lactuca sativa L.) polyphenol oxidase purification and characterization. J Agric Food Chem 49(10) 4870-4875. 

Wesche-Ebeling, P. and Montgomery, M.W. Strawberry polyphenol oxidase Purification and characterization, J. Food Sci., 55, 1315, 1990. 

Gandia-Herrero, R, Garefa-Carmona, R, and Escribano, J., Purification and characterization of a latent polyphenol oxidase from beet root Beta vulgaris L.), J. Agric. Food Chem., 52, 609, 2004. 

Cabanes J, Escribano J, Gandia-Herrero F, Garcia-Carmona F nd Jimenez-Atienzar M. 2007. Partial purification of latent polyphenol oxidase from peach (Prumis persica L. Cv. Catherina). Molecular properties and kinetic characterization of soluble and membrane-bound forms. J Agric Food Chem 55(25) 10446-10451. 

Perez-Gilabert M, Morte A, Honrubia M and Garcia-Carmona F. 2001. Partial purification, characterization, and histochemical localization of fully latent desert truffle (Terfezia claveryi Chatin) polyphenol oxidase. J Agric Food Chem 49(4) 1922-1927. 

Sajo M Mar, Nunez-Delicado E, Garcia-CarmonaF, Sanchez-Ferrer A. Partial purification of a bannana polyphenol oxidase using Triton X-l 14 and PEG 800G for removal of polyphenols. J Agric Food Chem 1998 46 4924-4930. 

Moore NL, Mariam DH, Williams AL, Dashek WV. Substrate specificity, de novo synthesis and partial purification of polyphenol oxidase derived from the wood-decay fungus, Coriolus versicolor. J Indust Microbiol 1989 4 349-364. 

Zawistowski, J., Biliaderis, C.G., and Murray, E.D., Purification and characterization of Jerusalem artichoke (Helianthus tuberosus L.) polyphenol oxidase, Food Biochem., 12, 1-22, 1988a. 

Many chemical reactions carried out in supercritical fluid media were discussed in the first edition, and those developments are included in total here after some recent work is described. In the epilogue (chapter 13) of the first edition we made reference to one of the author s work in enzyme catalyzed reactions in supercritical fluids that was (then) soon to appear in the literature. The paper (Hammond et al., 1985) was published while the first edition was in print, and as it turned out, there was a flurry of other activity in SCF-enzyme catalysis many articles describing work with a variety of enzymes, e.g., alkaline phosphatase, polyphenol oxidase, cholesterolase, lipase, etc., were published starting in mid 1985. Practical motivations were a potentially easier workup and purification of a product if the solvent is a gas (i.e., no liquid solvent residues to contend with), faster reaction rates of compounds because of gas-like transport properties, environmental advantages of carbon dioxide, and the like. 

Study of naturally-occurring enzyme inhibitors is of importance for several reasons. These include (a) the physiological importance of an inhibitor in biological material, (b) the nutritional importance of an inhibitor when the material is consumed as a food or feed, (c) the use of inhibitors to control enzymatic action, such as that of polyphenol oxidase, (d) the use of inhibitors for analysis and for purification purposes and (e) a better understanding of specific interactions among complex molecules such as proteins (examples include antigen-antibody reactions, subunit interactions in proteins, enzymatic actions). 

Erat, M., Sakiroglu, H., and Kufrevioglu, O.I. Purification and characterization of polyphenol oxidase... 

Tyrosinase is an enzyme complex (phenolase, polyphenol oxidase are other names which have been used for this enzyme), which catalyses of the ortho hydroxylation of monohydric phenols. The enzyme, which should not be confused with L-tyrosine hydroxylase mentioned above, contains Cu (I) and catalyses two distinct reactions—the hydroxylation of monohydric phenols to o-diphenols (cresolase activity) and the oxidation of o-diphenols to o-quinones (catecholase or catechol oxidase activity) . Most enzymes of this type, which are widely distributed in both the plant and animal kingdoms, exhibit both cataljrtic functions. Thus typically, the conversion of L-tyrosine (5) to L-dopa (15) and dopaquinone (36) which occurs in melanin biosynthesis is catalysed by an enzyme of the tyrosinase category. The two activities appear, in the majority of cases, to be functions of the same enzyme. However, certain o-diphenol oxidases such as those from tea , sweet potato and tobacco have been reported to show no capacity to catalyse the hydroxylation reaction but this is most probably due to destruction of the cresolase activity during purification. 

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