Evaluating the antioxidant capacity of wines: a laccase-based biosensor approach

Gil, Dulce M. A.; Rebelo, M. J. F.

doi:10.1007/s00217-010-1280-0

Cited by 38 publications

(27 citation statements)

References 30 publications

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“…Several amperometric biosensors for the detection of phenolic compounds have been developed, on the basis of enzymes, such as tyrosinase, laccase or peroxidase [106][107][108][109]. Biosensors for phenolic compounds were constructed by immobilizing polyphenol oxidase (PPO) into conducting copolymers prepared by electropolymerization of pyrrole with thiophene capped polytetrahydrofuran [108].…”

Section: Biosensors Methodsmentioning

confidence: 99%

Methods for Total Antioxidant Activity Determination: A Review

Pisoschi¹,

Negulescu²

2012

Biochem & Anal Biochem

330

302

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Section: Biosensors Methodsmentioning

confidence: 99%

Methods for Total Antioxidant Activity Determination: A Review

Pisoschi¹,

Negulescu²

2012

Biochem & Anal Biochem

330

302

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“…Actually, the assay based on Folin-Ciocalteu reagent and (commonly known as the total phenolic assay) measures a sample's reducing capacity, and therefore the obtained results should be considered as the content of all reducing substances in the herbal infusion, and not exclusively considering the phenolic content (Wang, Chang, Inbaraj, & Chen, 2010). Furthermore, the BPI values depend on the standard phenolic compound taken as the biosensing reference (Gamella et al, 2006;Gil & Rebelo, 2010).…”

Section: Polyphenolic Contents Of Herbal Infusions and Tea Samplesmentioning

confidence: 99%

“…A large number of amperometric biosensors has been seen and proposed as attractive, alternative analytical methods for the quantification of phenolic compounds (Abhijith, Sujith, Kumar, & Thakur, 2007;Arecchia, Scampicchioa, Druschb, & Mannino, 2010;Girelli, Mattei, & Papaleo, 2009;Mello, Alves, Macedo, & Kubota, 2005) since they are characterised by their inherent specificity, simplicity and fast response, with most of them being based on the immobilisation of laccase on different electrode supports (Elkaoutit et al, 2008;Gamella, Campuzano, Reviejo, & Pingarrón, 2006;Gil & Rebelo, 2010;Ibarra-Escutia, Gómeza, Calas-Blanchard, Marty, & Ramírez-Silva, 2010;Montereali, Seta, Vastarella, & Pilloton, 2010).…”

Section: Introductionmentioning

confidence: 99%

Herbal infusions bioelectrochemical polyphenolic index: Green tea – The gallic acid interference

et al. 2011

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“…However, laccase is currently prohibited as a food additive; thus, its application necessitates the use of an immobilized form that allows its removal, thereby complicating widespread commercial use in food processing 1. 34, 35…”

Section: Applications Of Laccasesmentioning

confidence: 99%

Stabilized Laccases as Heterogeneous Bioelectrocatalysts

Betancor

Johnson²,

Luckarift

2012

ChemCatChem

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Typically, the use of heterogeneous enzyme catalysis is aimed at sustainability, reusability, or enhanced functionality of the biocatalyst and is achieved by immobilizing enzymes onto a support matrix or at a defined interface. Controlled enzyme immobilization is particularly important in bioelectrocatalysis because the catalyst must be effectively connected to a transducer to exploit its activity. This Review discusses what must be addressed for coupling biocatalysts to an electrode and the toolbox of methods that are available for achieving this outcome. As an illustration, we focus on the immobilization and stabilization of laccases at electronic interfaces. Historically, laccases have been used for the decolorization of dyes and for the synthesis of bio‐organic compounds; however, more recently, they have been applied to the fields of sensing and energy harvesting.1–3 There is an ever‐increasing focus on the development of new energy technologies, in which laccases find application (e.g., as cathodic catalysts in enzymatic fuel cells). Herein, we discuss the heterogeneous laccase biocatalysts that have been reported over the past 10–15 years and discuss why laccases continue to be biotechnologically relevant enzymes. Various methods for the immobilization of laccases are described, including the use of nanoscale supports and a range of encapsulation and cross‐linking chemistries. We consider the application of immobilized laccases to the food industry, in the synthesis of pharmaceuticals, and in environmental applications, specifically in cases in which stabilization through heterogenization of the enzyme is critical to the application. We also include a consideration of electrochemical biosensors and the specific incorporation of laccases on the surfaces of transducers.

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Evaluating the antioxidant capacity of wines: a laccase-based biosensor approach

Cited by 38 publications

References 30 publications

Methods for Total Antioxidant Activity Determination: A Review

Methods for Total Antioxidant Activity Determination: A Review

Herbal infusions bioelectrochemical polyphenolic index: Green tea – The gallic acid interference

Stabilized Laccases as Heterogeneous Bioelectrocatalysts

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