First extraction of polyphenol oxidase from edible desert truffle (Terfezia leonis Tul.) and its thermal behavior

Gouzi, Hicham; Depagne, Christophe; Benmansour, Abdelhafid; Coradin, Thibaud

doi:10.1007/s00217-013-2040-8

Cited by 12 publications

(8 citation statements)

References 34 publications

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“…[49] Positive DS Ã at pH 5.7 appears to suggest unfolding of protein. A similar observation was reported by Gouzi et al [50] The entropy change is maximal at pH 5.7. The isoelectric point of the enzyme is 4.8 (experimental details not given).…”

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confidence: 76%

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Optimization of Laccase Fermentation and Evaluation of Kinetic and Thermodynamic Parameters of a Partially Purified Laccase Produced byDaedalea flavida

Singha¹,

Panda²

2014

Preparative Biochemistry and Biotechnology

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Studies on laccase production by Daedalea flavida were carried out in static and low-speed shake cultures. The enzyme production was reduced drastically at a high speed of shaking. Optimal production conditions are necessary to assess the quality of laccase suitable for a specific application. Thus, the production of laccase was optimized by the application of response surface methodology. Laccase production was 8-fold and 7.5-fold more in static and low-speed shake conditions, respectively, in an optimal medium composition than in an unoptimized medium. Laccase obtained using the optimal culture medium of D. flavida was tested for its stability at different temperatures and pH conditions. The partially purified enzyme was most stable at 30°C and pH 5. The half-life of laccase is 87 min at 60°C and at pH 6. The kinetic and thermodynamic parameters were evaluated for the inactivation of the partially purified laccase. The entropy change of inactivation of the enzyme is least at pH 4.

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confidence: 76%

“…Five different incubation 20,30,40,50, and 60 C, were used to study the effect of temperature. At each incubation temperature, five different values of pH (4, 4.3, 5, 5.7, and 5.99) were adjusted in the enzyme solution to study the effect of pH.…”

Section: Fermentation Conditions Used In the Plackett-burman Design Amentioning

confidence: 99%

Optimization of Laccase Fermentation and Evaluation of Kinetic and Thermodynamic Parameters of a Partially Purified Laccase Produced byDaedalea flavida

Singha¹,

Panda²

2014

Preparative Biochemistry and Biotechnology

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“…In agreement with other literature, PPO sources and substrates have different optimum and unstable temperatures. For example, the optimum temperature was 30°C for Desert truffle using catechol as a substrate (Hicham, Christophe, Abdelhafid, &Thibaud, 2013), and 40°C for Honeydew peach using catechol as substrate (Liu, Cao, Yang, & Qi, 2015). The thermostability of yam PPO was similar to the results of apricot PPO, which loses more than 90% of its activity after incubation at 70°C for 10 min (Derardja, Pretzler, Kampatsikas, Barkat, & Rompel, 2011).…”

Section: Ph Optimum Temperature Optimum and Thermostabilitymentioning

confidence: 63%

Purification and characterization of polyphenol oxidase (PPO) from water yam (Dioscorea alata)

Peng

et al. 2019

CyTA - Journal of Food

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Polyphenol oxidase (PPO) is responsible for the enzymatic browning of fruits and vegetables, and thus has negative effects on the quality of food. In this study, extraction and purification of PPO from water yam was performed successfully, and the characteristics of PPO and inhibitors of enzyme activity were analysed. The results showed that PPO activity improved by 4.58-fold through the DEAE-Sepharose and Superdex G-75 purification technique, which reached electrophoretic purity. The enzyme molecular weight was estimated to be 32 kDa. The optimum pH and temperature values of PPO were 6.0 and 35°C, respectively, and it was not thermostable at higher temperatures. PPO had the highest substrate affinity towards catechol (Km = 27.82 mmol/L and Vmax = 1.464 △A/ min). The most effective inhibitor was L-cysteine followed by ascorbic acid and sodium sulfite. Purificación y caracterización de la polifenol oxidasa (PPO) obtenida del ñame de agua (Dioscorea alata) RESUMEN La polifenol oxidasa (PPO) es responsable del pardeamiento enzimático de frutas y verduras; por lo tanto, tiene efectos negativos en la calidad de los alimentos. En el presente estudio se extrajo y se purificó con éxito la PPO proveniente del ñame de agua, y se analizaron sus características y los inhibidores de la actividad enzimática. En este sentido, los resultados indicaron que la actividad de la PPO mejoró 4.58 veces al emplear la técnica de purificación DEAE-Sepharose y Superdex G-75, que alcanzó la pureza electroforética. El peso molecular de la enzima se estimó en 32 kDa. Los valores óptimos de pH y temperatura de la PPO fueron 6.0 y 35°C, respectivamente, constatándose que no era termoestable a temperaturas más altas. La PPO mostró mayor afinidad de sustrato hacia el catecol (Km = 27.82 mmol/L y Vmax = 1.464 △A/min). Su inhibidor más efectivo fue la L-cisteína, seguida por el ácido ascórbico y el sulfito de sodio.

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“…for tyrosinase extraction were obtained from Algerian Southern. The protocol for extraction was described by Gouzi et al [28]. First, 50 g of peridium from truffles were homogenized in 100 mL of 0.05 M phosphate buffer (pH 7.0), using a Waring blender for 2 min.…”

Section: Extraction Of Tyrosinasementioning

confidence: 99%

An optical catechol biosensor based on a desert truffle tyrosinase extract immobilized into a sol–gel silica layered matrix

Leboukh

Gouzi

Coradin

et al. 2018

J Sol-Gel Sci Technol

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optical catechol biosensor based on a desert truffle tyrosinase extract immobilized into a sol-gel silica layered matrix. AbstractAn optical biosensor for the determination of catechol, a widely used yet toxic and carcinogenic molecule, is proposed using a crude extract of desert truffle (Terfezia leonis Tul.)as an enzymatic source of tyrosinase. The biosensor is constructed by the immobilization of tyrosinase crude extract in a bi-layered silica gel film prepared by dip-coating of an alkoxide/colloidal silica solution containing the enzyme on glass slide. Encapsulation has a moderate effect of the enzyme optimal pH stability but largely increases its thermal stability.Immobilized enzymes have a higher substrate affinity towards catechol but smaller maximum conversion velocity. The optical biosensor provides a linear response for catechol in the concentration range of 50-400 µM and a limit of detection was 52 µM. AFM studies show that the enzymes impact on the silica gel structure, preventing further deposition of additional layers. Comparison with similar dopamine biosensors points out that the impact of encapsulation on enzymatic activity may depend on the considered substrate.

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First extraction of polyphenol oxidase from edible desert truffle (Terfezia leonis Tul.) and its thermal behavior

Cited by 12 publications

References 34 publications

Optimization of Laccase Fermentation and Evaluation of Kinetic and Thermodynamic Parameters of a Partially Purified Laccase Produced byDaedalea flavida

Optimization of Laccase Fermentation and Evaluation of Kinetic and Thermodynamic Parameters of a Partially Purified Laccase Produced byDaedalea flavida

Purification and characterization of polyphenol oxidase (PPO) from water yam (Dioscorea alata)

An optical catechol biosensor based on a desert truffle tyrosinase extract immobilized into a sol–gel silica layered matrix

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