Die Chemie der Proteinoxidation in Lebensmitteln

Hellwig, Michael

doi:10.1002/ange.201814144

Cited by 2 publications

(3 citation statements)

References 284 publications

(709 reference statements)

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“…Probably the most widely used routine method for protein oxidation measurement is the determination of carbonyl groups that react with 2,4-dinitrophenylhydrazine (DNPH) to form the corresponding hydrazones, which are then quantified spectrophotometrically. Carbonyl compounds not related to protein oxidation may be formed during lipid peroxidation and the Maillard reaction leading to an overestimation of protein oxidation [14]. Another commonly used method to assess oxidative changes in meat is the determination of thiol groups in meat [14][15][16][17][18][19][20].…”

Section: Introductionmentioning

confidence: 99%

“…Carbonyl compounds not related to protein oxidation may be formed during lipid peroxidation and the Maillard reaction leading to an overestimation of protein oxidation [14]. Another commonly used method to assess oxidative changes in meat is the determination of thiol groups in meat [14][15][16][17][18][19][20]. Free thiol groups may be analyzed by spectrophotometric after derivatization with Ellman's reagent 86 (5,5 -dithio-bis(2-nitrobenzoic acid) (DTNB)), which leads to the formation of a mixed disulfide and release of 5-thio-2-nitrobenzoic acid.…”

Section: Introductionmentioning

confidence: 99%

“…Free thiol groups may be analyzed by spectrophotometric after derivatization with Ellman's reagent 86 (5,5 -dithio-bis(2-nitrobenzoic acid) (DTNB)), which leads to the formation of a mixed disulfide and release of 5-thio-2-nitrobenzoic acid. Contrarily to the DNPH method, the spectrophotometric method using Ellman's reagent does not require solubility of the protein, but can be applied in suspension [14].…”

Section: Introductionmentioning

confidence: 99%

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Prediction of Thiol Group Changes in Minced Raw and Cooked Chicken Meat with Plant Extracts—Kinetic and Neural Network Approaches

Kaczmarek

Muzolf-Panek

2021

Animals

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The aim of the study was to develop predictive models of thiol group (SH) level changes in minced raw and heat-treated chicken meat enriched with selected plant extracts (allspice, basil, bay leaf, black seed, cardamom, caraway, cloves, garlic, nutmeg, onion, oregano, rosemary, and thyme) during storage at different temperatures. Meat samples with extract addition were stored under various temperatures (4, 8, 12, 16, and 20 °C). SH changes were measured spectrophotometrically using Ellman’s reagent. Samples stored at 12 °C were used as the external validation dataset. SH content decreased with storage time and temperature. The dependence of SH changes on temperature was adequately modeled by the Arrhenius equation with average high R2 coefficients for raw meat (R2 = 0.951) and heat-treated meat (R2 = 0.968). Kinetic models and artificial neural networks (ANNs) were used to build the predictive models of thiol group decay during meat storage. The obtained results demonstrate that both kinetic Arrhenius (R2 = 0.853 and 0.872 for raw and cooked meat, respectively) and ANN (R2 = 0.803) models can predict thiol group changes in raw and cooked ground chicken meat during storage.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Prediction of Thiol Group Changes in Minced Raw and Cooked Chicken Meat with Plant Extracts—Kinetic and Neural Network Approaches

Kaczmarek

Muzolf-Panek

2021

Animals

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What Determines the Selectivity of Arginine Dihydroxylation by the Nonheme Iron Enzyme OrfP?

Ali

Henchman

Visser

2020

Chemistry A European J

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The nonheme iron enzyme OrfP reacts with l‐Arg selectively to form the 3R,4R‐dihydroxyarginine product, which in mammals can inhibit the nitric oxide synthase enzymes involved in blood pressure control. To understand the mechanisms of dioxygen activation of l‐Arg by OrfP and how it enables two sequential oxidation cycles on the same substrate, we performed a density functional theory study on a large active site cluster model. We show that substrate binding and positioning in the active site guides a highly selective reaction through C3−H hydrogen atom abstraction. This happens despite the fact that the C3−H and C4−H bond strengths of l‐Arg are very similar. Electronic differences in the two hydrogen atom abstraction pathways drive the reaction with an initial C3−H activation to a low‐energy 5σ‐pathway, while substrate positioning destabilizes the C4−H abstraction and sends it over the higher‐lying 5π‐pathway. We show that substrate and monohydroxylated products are strongly bound in the substrate binding pocket and hence product release is difficult and consequently its lifetime will be long enough to trigger a second oxygenation cycle.

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Die Chemie der Proteinoxidation in Lebensmitteln

Cited by 2 publications

References 284 publications

Prediction of Thiol Group Changes in Minced Raw and Cooked Chicken Meat with Plant Extracts—Kinetic and Neural Network Approaches

Prediction of Thiol Group Changes in Minced Raw and Cooked Chicken Meat with Plant Extracts—Kinetic and Neural Network Approaches

What Determines the Selectivity of Arginine Dihydroxylation by the Nonheme Iron Enzyme OrfP?

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