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Stereospecificity of Mushroom Tyrosinase Immobilized on a Chiral and a Nonchiral Support

Marín-Zamora, María Elisa ; Rojas-Melgarejo, Francisco ; García-Cánovas, Francisco ; García-Ruiz, Pedro Antonio

Journal of agricultural and food chemistry, 2007-05, Vol.55 (11), p.4569-4575 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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Título:
Stereospecificity of Mushroom Tyrosinase Immobilized on a Chiral and a Nonchiral Support
Autor: Marín-Zamora, María Elisa ; Rojas-Melgarejo, Francisco ; García-Cánovas, Francisco ; García-Ruiz, Pedro Antonio
Assuntos: Agaricus bisporus ; Biological and medical sciences ; catechol oxidase ; chemical analysis ; enantiomers ; enzyme activity ; enzyme inactivation ; enzyme inhibition ; enzyme kinetics ; Enzymes, Immobilized - chemistry ; extraction ; Food engineering ; Food industries ; Fruit and vegetable industries ; Fundamental and applied biological sciences. Psychology ; General aspects ; glycerine cinnamate ; Kinetics ; Monophenol Monooxygenase - chemistry ; mushrooms ; sorbitol cinnamate ; stereochemistry ; Stereoisomerism ; Substrate Specificity
É parte de: Journal of agricultural and food chemistry, 2007-05, Vol.55 (11), p.4569-4575
Notas: http://dx.doi.org/10.1021/jf0701178
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Descrição: Mushroom tyrosinase was immobilized from an extract onto glass beads covered with the cross-linked totally cinnamoylated derivates of d-sorbitol (sorbitol cinnamate) and glycerine (glycerine cinnamate). The enzyme was immobilized onto the support by direct adsorption, and the quantity of immobilized tyrosinase was higher for sorbitol cinnamate, the support with the higher number of esterified hydroxyls per unit of monosacharide, than for glycerine cinnamate. The results obtained from the stereospecificity study of the monophenolase and diphenolase activity of immobilized mushroom tyrosinase are reported. The enantiomers l-tyrosine, dl-tyrosine, d-tyrosine, l-dopa, dl-dopa, d-dopa, l-α-methyldopa, dl-α-methyldopa, l-isoprenaline, dl-isoprenaline, l-adrenaline, dl-adrenaline, l-noradrenaline, and d-noradrenaline were assayed with tyrosinase immobilized on a chiral support (sorbitol cinnamate), whereas l-tyrosine, dl-tyrosine, d-tyrosine, l-dopa, dl-dopa, d-dopa, l-α-methyldopa, and dl-α-methyldopa were assayed with tyrosinase immobilized on a nonchiral support (glycerine cinnamate). The same values for each series of enantiomers were obtained. However, the values were different, the l isomers showing lower values than the dl isomers, whereas the highest value was obtained with d isomers. No difference was observed in the stereospecificity of tyrosinase immobilized on a chiral (sorbitol cinnamate) or nonchiral (glycerine cinnamate) support. Keywords: Mushroom tyrosinase; immobilization; cinnamic carbohydrate esters; tyrosinase extraction; enzyme kinetics; stereospecificity
Editor: Washington, DC: American Chemical Society
Idioma: Inglês

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Stereospecificity of Mushroom Tyrosinase Immobilized on a Chiral and a Nonchiral Support

Marín-Zamora, María Elisa ; Rojas-Melgarejo, Francisco ; García-Cánovas, Francisco ; García-Ruiz, Pedro Antonio

Washington, DC: American Chemical Society

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