Cinnamic ester of <scp>D</scp>‐sorbitol for immobilization of mushroom tyrosinase

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

doi:10.1002/jctb.1334

Cited by 17 publications

(19 citation statements)

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“…4). Similar results leading to thermal stability and distinct lowering in pH in the system's macro environment caused by the incorporation of additional positive charges were obtained in case of immobilization of tyrosinase on D-cinnamic sorbitol esters by adsorption [30] as well as in the reversible tyrosinase immobilization on polyethyleneimine-grafted and Cu (II)- chelated poly(HEMA-co-GMA)-reactive membranes [31].…”

Section: Discussionsupporting

confidence: 59%

Performance evaluation of a silk protein‐based matrix for the enzymatic conversion of tyrosine to L‐DOPA

Acharya

Kumar

Sen

et al. 2008

Biotechnology Journal

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L-DOPA (3,4-dihydroxyphenyl-L-alanine), one of the most important intermediates in the melanin biosynthesis pathway, is used for the treatment of Parkinson's disease. With a view of developing a cheaper and more effective method for the bioconversion of tyrosine to L-DOPA, the potential and performance of a novel fibrous matrix prepared from Bombyx mori silk protein fibroin were evaluated for the immobilization of tyrosinase. Cross-linkage between fibroin and tyrosinase using glutaraldehyde was evident from Fourier transform infra red spectroscopy. Maximum product formation occurred when 1000 U enzyme was immobilized on 20 mg fibroin. The optimum conditions for maximal L-DOPA production using immobilized tyrosinase were 40 degrees C and pH 5.5, conditions that caused a 50% loss of free enzyme activity. Immobilized tyrosinase also showed to have a higher degree of stability during storage and it retained 80% of its original activity after repeated reuses. The efficiency of this immobilized tyrosinase system to produce L-DOPA was high, as evident from a high effectiveness factor, between 0.7 and 0.8, thereby making this method feasible for the large-scale production of L-DOPA.

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Section: Discussionsupporting

confidence: 59%

Performance evaluation of a silk protein‐based matrix for the enzymatic conversion of tyrosine to L‐DOPA

Acharya

Kumar

Sen

et al. 2008

Biotechnology Journal

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“…PPD is important as it is responsible for eye, skin, inner ear and hair melanization, as well as browning in fruits and vegetables (Marín-Zamora et al, 2005). Particularly, when a plant gets a damage, cut or bruise, a polymer structure is formed by the the enzyme which oxidizes some phenolic compounds, thus resulting in protection of the plant against microorganisms or insects ( Van Gelder et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of polyphenol oxidase from purslane

Güven

Bekler

et al. 2017

Food Sci. Technol

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The polyphenol oxidase (PPD) is an enzyme that is responsible for the enzymatic browning of fruits and vegetables. This is generally undesired process and need to be prevented in food technology. PPD from purslane was purified, characterised and the kinetic parameters for three substrates namely, catechol, L-Dopa and 4-methylcatechol were determined. The optimum pH and temperature values were found to be pH 7.0 and 50 °C, respectively using the catechol as substrate. The apparent molecular weight of the PPD from purslane was determined as high as 163 kDa by partially denaturing SDS-PAGE. Moreover, the inhibition kinetics of the purified PPD were determined, using both synthetic and natural inhibitors. Among inhibitors tested, ascorbic acid was the most effective inhibitor with the lowest Ki value of 0.36 mM. This is the first study on the purification and characterisation of PPD from purslane (Portulaca oleracea) that may provide new insight into how to overcome the enzymatic browning.Keywords: Portulaca oleracea; polyphenol oxidase; purification; kinetics; inhibitors.Practical Applications: Understanding inhibition mechanism of PPD may provide insight into plant browning in food industry.

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“…The hexacinnamate of d-sorbitol was characterized in previous works (Marín-Zamora et al, 2005;Rojas-Melgarejo et al, 2004a) from various experimental analyses: 1 H NMR and 13 C NMR, distortionless enhancement by polarization transfer (DEPT) spectra, different two-dimensional experiments (COSY and C/H ratio) and infrared spectra of the prepared compound. In the present work total esterification was confirmed by 1 H NMR and 13 C NMR.…”

Section: Photoreactive Prepolymers Preparationmentioning

confidence: 99%