Production of o-diphenols by immobilized mushroom tyrosinase

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

doi:10.1016/j.jbiotec.2008.10.014

Cited by 37 publications

(23 citation statements)

References 34 publications

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“…Aberg et al [129] used tyrosinase for biocatalytic grafting of phenolic moieties or protein onto chitosan. Production of o -diphenols was done using mushroom tyrosinase from Agaricus bisporus which was immobilized on commercially available epoxy-resin EupergitC250L and then coated using layer-by-layer method (LbL) [167]. The two novel heterogeneous biocatalysts have been characterized for their morphology and reusability.…”

Section: Other Applicationsmentioning

confidence: 99%

Microbial Tyrosinases: Promising Enzymes for Pharmaceutical, Food Bioprocessing, and Environmental Industry

Zaidi

Ali²,

Ali³

et al. 2014

Biochemistry Research International

145

111

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Tyrosinase is a natural enzyme and is often purified to only a low degree and it is involved in a variety of functions which mainly catalyse the o-hydroxylation of monophenols into their corresponding o-diphenols and the oxidation of o-diphenols to o-quinones using molecular oxygen, which then polymerizes to form brown or black pigments. The synthesis of o-diphenols is a potentially valuable catalytic ability and thus tyrosinase has attracted a lot of attention with respect to industrial applications. In environmental technology it is used for the detoxification of phenol-containing wastewaters and contaminated soils, as biosensors for phenol monitoring, and for the production of L-DOPA in pharmaceutical industries, and is also used in cosmetic and food industries as important catalytic enzyme. Melanin pigment synthesized by tyrosinase has found applications for protection against radiation cation exchangers, drug carriers, antioxidants, antiviral agents, or immunogen. The recombinant V. spinosum tryosinase protein can be used to produce tailor-made melanin and other polyphenolic materials using various phenols and catechols as starting materials. This review compiles the recent data on biochemical and molecular properties of microbial tyrosinases, underlining their importance in the industrial use of these enzymes. After that, their most promising applications in pharmaceutical, food processing, and environmental fields are presented.

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Section: Other Applicationsmentioning

confidence: 99%

Microbial Tyrosinases: Promising Enzymes for Pharmaceutical, Food Bioprocessing, and Environmental Industry

Zaidi

Ali²,

Ali³

et al. 2014

Biochemistry Research International

145

111

View full text Add to dashboard Cite

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“…Kinetic studies were carried out in glass vials by incubating 0.2 g matrix capsules (5-60 mg cdw/(ml polymer solution), N ≈ 200, r = 0.6 mm unless otherwise stated) with 3.8 ml BPA solution (2.1-438 mol/l) with a certain pH value (3)(4)(5)(6)(7)(8)(9)(10)(11) adjusted to with HCl or NaOH. Due to the high water content of the matrix capsules it was assumed that the BPA was diluted rapidly to a 4% lower concentration (2-420 mol/l, see Section 3.1 for details), which is considered as the initial BPA concentration reported in Section 3.2.…”

Section: Reaction Kinetic Studiesmentioning

confidence: 99%

“…This reaction pattern has been examined for tyrosinase catalyzed production of various o-diphenols [3,4], among these the antioxidant hydroxytyrosol [5], 3,4-dihydroxyphenylacetic acid [4], a substance with antiproliferative activity against cancer cells [6], and 3,4-dihydroxy-l-phenylalanine (l-DOPA) [7][8][9] which is a prescribed drug for treatment of Parkinson's disease. The formation of the o-quinones in these reaction systems can be reduced by addition of ascorbic acid as a reducing agent [3][4][5][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

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Kinetic characterization of tyrosinase containing mushroom (Agaricus bisporus) cells immobilized in silica alginate

Kampmann

Hoffrichter

Stalinski

et al. 2015

Journal of Molecular Catalysis B: Enzymatic

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“…There are several studies already immobilizing enzymes (Arroyo, 1998;Datta et al, 2013, Kupferschmidt et al 2014), but only a few of them are made with PPO and mesoporous materials. Concretely, their purpose is far from the food industry, as they entrap PPO to detect phenolic compounds (Mangrulkar et al, 2012) or to produce o-diphenols in vitro (Marín-Zamora et al, 2009). …”

Section: Introductionmentioning

confidence: 99%

Application of mesoporous silica materials for the immobilization of polyphenol oxidase

et al. 2017

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Enzymatic browning is one of the most important reactions that occur in fruits and vegetables, resulting in negative effects on color, taste, flavour and nutritional value. The main agent responsible for this reaction is polyphenol oxidase (PPO), also called tyrosinase, because it oxidises phenolic compounds and generates dark pigments. Mesoporous materials have been popular for a variety of applications in the last two decades, such as catalysis and gas separation, and they are an interesting option to immobilize the PPO as an alternative to the established industry process based on heat treatments. The objective of the present work is to study the possibility to remove this enzyme or even inhibit its activity from apple juice, since this beverage is rich in polyphenols and it is susceptible to suffering enzymatic browning. Different mesoporous silica materials were tested with different structures, morphologies and porosities in order to see their influence on the immobilization rate. Besides, the pH value of the solution and time were fully analysed and they provide results to obtain a good immobilization capacity. Pore volume, is the textural characteristic which affects the most the immobilization assay. Aeroperl® and SBA-15 are the materials which can adsorb larger quantity of PPO at pH 4.00, because electrostatic interactions can exist between the enzyme and the silica walls. Fitting power law and Higuchi models, we can assume that the PPO loading into mesoporous materials is diffusion controlled. The commercial mesoporous material reveals highest inhibition rates in real apple extracts.KEYWORDS: mesoporous material, silica, tyrosinase, polyphenol oxidase, PPO, juice treatment, enzymatic browning. 2 RESUMENLa principal reacción que afecta tanto a frutas como a verduras y que causa un detrimento en su color, sabor, olor y valor nutricional es el pardeamiento enzimático. La polifenol oxidasa (PPO), también llamada tirosinasa, es la principal responsable de esta reacción, ya que oxida los compuestos fenólicos generando pigmentos parduzcos. Los materiales mesoporosos han tenido una gran variedad de aplicaciones en las últimas dos décadas, como por ejemplo catálisis y separación de gases, y estos materiales son una interesante opción para inmovilizar la PPO como alternativa a los tratamientos térmicos implementados en la industria. El objetivo de este trabajo es estudiar la posibilidad de retener este enzima o incluso inhibir su actividad aplicándolo sobre zumo de manzana, puesto que, como esta bebida es rica en compuestos fenólicos, es más susceptible de sufrir esta reacción de pardeamiento. Para ello, se han estudiado diferentes materiales mesoporosos de sílice con diferentes estructuras, morfologías y porosidades para poder dilucidar su influencia en la tasa de inmovilización. Además, otros factores que han sido ampliamente estudiados han sido la influencia del pH de la solución de inmovilización y el tiempo de contacto entre el material y el enzima. La característica textural que parece ser decisi...

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Production of o-diphenols by immobilized mushroom tyrosinase

Cited by 37 publications

References 34 publications

Microbial Tyrosinases: Promising Enzymes for Pharmaceutical, Food Bioprocessing, and Environmental Industry

Microbial Tyrosinases: Promising Enzymes for Pharmaceutical, Food Bioprocessing, and Environmental Industry

Kinetic characterization of tyrosinase containing mushroom (Agaricus bisporus) cells immobilized in silica alginate

Application of mesoporous silica materials for the immobilization of polyphenol oxidase

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