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Arda Serpen

Researcher at Hacettepe University

Publications -  36
Citations -  3151

Arda Serpen is an academic researcher from Hacettepe University. The author has contributed to research in topics: ABTS & Acrylamide. The author has an hindex of 27, co-authored 36 publications receiving 2736 citations. Previous affiliations of Arda Serpen include Spanish National Research Council.

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A new procedure to measure the antioxidant activity of insoluble food components.

TL;DR: Alkali hydrolysis reduced up to 90% the antioxidant activity of cereal-based insoluble matters, thus confirming that fiber-bound compounds have a major role in their antioxidant activity.
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Phenolic Compounds, Carotenoids, Anthocyanins, and Antioxidant Capacity of Colored Maize (Zea mays L.) Kernels

TL;DR: The light blue ZPP-2 selfed maize genotype has a higher content of total phenolics, flavonoids, and ferulic acid as compared to other tested maize and the highest ABTS radical scavenging activity.
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Study of lipoxygenase and peroxidase as indicator enzymes in green beans: change of enzyme activity, ascorbic acid and chlorophylls during frozen storage

TL;DR: In this article, the effects of two blanching conditions using peroxidase (POD) and lipoxygenase (LOX) as indicator enzyme on residual enzyme activities, ascorbic acid and chlorophyll content in green beans during frozen storage were studied.
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Direct measurement of the total antioxidant capacity of foods: the ‘QUENCHER’ approach

TL;DR: In this paper, a review of the solubility and localization of food antioxidant compounds was provided as base to understand the advantage of the direct procedure with respect to the extraction protocols present in the literature.
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Total antioxidant capacities of raw and cooked meats.

TL;DR: The QUENCHER procedure, which is performed directly on the solid material without extraction, was selected and proved to be particularly suitable for meat samples and the modifications of TAC during cooking can be explained considering factors such as denaturation and exposure of reactive protein sites.