Interaction of benzyl isothiocyanate with egg white proteins

Kroll, J.; Rawel, Harshadrai M.; Kröck, R.; Schnaak, W.

doi:10.1002/food.19930370215

Cited by 7 publications

(9 citation statements)

References 8 publications

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“…Polymerisation of protein molecules (ovalbumin, insulin and BSA) after reaction with allyl-ITC has also been reported [16]. Experiments with egg white proteins also showed polymerization reaction with different types of ITC [l,2,IS]. A similar but a much more pronounced protein polymerization in the derivative was also observed when the SDS-PAGE was performed only in presence of SDS, that is, the disulfide bridges remained intact (Fig.…”

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Some aspects of reactions of benzyl isothiocyanate with bovine sarcoplasmic proteins

Rawel¹,

Kroll²

1995

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Benzyl-ITC (benzyl isothiocyanate) reacts preferentially with amino groups and sulfhydryl side chains of bovine sarcoplasmic proteins to form thiourea and dithiocarbamate derivatives, generally resulting in a decrease in solubility of the derivatives along a wide pH range. Under these conditions, it was also possible to show that secondary amine side chains, as found in tryptophan, also react with benzyl-ITC. A quenching of tryptophan fluorescence intensity after interaction with benzyl-ITC was also observed. Polyacrylamide gel electrophoresis (PAGE) experiments in the presence of urea indicated changes in electrophoretical mobility and in composition of subfractions. Changes in surface hydrophobicity and composition as determined by the ANS (8-anilinonaphthalene-1-sulfonate) method and RP-HPLC were also observed. Polymerisation of protein molecules after reaction with benzyl-ITC was documented using the SDS-PAGE technique. These investigations showed that a group of subfractions belonging mainly to glycolytic enzymes and associated proteins with molecular weight between 38-70 kDa was highly reactive.

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Some aspects of reactions of benzyl isothiocyanate with bovine sarcoplasmic proteins

Rawel¹,

Kroll²

1995

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“…(2011) demonstrated that in a first step isothiocyanates react with the thiols that are present, and amino groups are only modified in excess concentrations of the isothiocyanates 172. The release of carbon disulfide from those proteins functions as a marker for the formation of dithiocarbamate (and its further degradation), as shown for egg white proteins and the enzyme bromelain from pineapple ( Ananas comosus ) 166a. 170a Furthermore, Kawakishi and Kaneko (1987) studied the reactions of isothiocyanate 31 with several food proteins at pH values of 6–7.5.…”

Section: Reactivity Of Glucosinolate Breakdown Productsmentioning

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Reactivity and Stability of Glucosinolates and Their Breakdown Products in Foods

et al. 2014

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The chemistry of glucosinolates and their behavior during food processing is very complex. Their instability leads to the formation of a bunch of breakdown and reaction products that are very often reactive themselves. Although excessive consumption of cabbage varieties has been thought for long time to have adverse, especially goitrogenic effects, nowadays, epidemiologic studies provide data that there might be beneficial health effects as well. Especially Brassica vegetables, such as broccoli, radish, or cabbage, are rich in these interesting plant metabolites. However, information on the bioactivity of glucosinolates is only valuable when one knows which compounds are formed during processing and subsequent consumption. This review provides a comprehensive, in-depth overview on the chemical reactivity of different glucosinolates and breakdown products thereof during food preparation.

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“…Recently we reported about interactions of benzyl-ITC with egg white proteins, documented by reactions with amino groups as well as with sulphhydryl side chains of proteins [8].…”

Section: Introductionmentioning

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Interactions of isothiocyanates with egg white proteins

Kroll¹,

Rawel²,

Kröck³

et al. 1994

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SummaryGlucosinolates and their very highly reactive breakdown products (mainly isothiocyanates = ITC) belong to one of the most important natural toxicants. This paper deals with the interactions of allyl-, butyl-, phenyl-and benzyl ITC with egg white proteins resulting in the formation of ITC-proteinconjugates. The ITC's react with amino groups by forming thiourea derivatives. Such reactions are well described by changes in the amounts of free amino groups and available lysine. Further reaction sites are sulphhydryl side chains of proteins leading to dithiocarbamate esters. The investigations further show that such reactions are accompanied with a decrease in the solubility of the prepared conjugates. Simultaneously a shift of the isoelectric range to a lower value of pH can also be observed. Changes in electrophoretic patterns and mobility can also be seen due to the strong electrophilic attack of ITC to proteins. Comparison of the 4 investigated preparations shows that benzyl-ITC is the most reactive partner for egg white proteins. ZusammenfassungGlucosinolate und ihre reaktiven Spaltprodukte (hauptsachlich Isothiocyanate = ITC) zahlen zu den wichtigsten natiirlichen Schadstoffen. Wie gezeigt wird, fiihren Wechselwirkungen von Allyl-, Butyl-, Benzyl-und Phenyl-ITC mit Eiklarproteinen (frisches Eiklar) zur Bildung von ITC-ProteinKonjugaten. Die ITC reagierenmit Aminogruppen unter Bildung von Thioharnstoff-Derivaten. Diese Reaktionen lassen sich iiber Anderungen (Abnahme) im Gehalt an freien Aminogruppen und an verfiigbarem Lysin gut beschreiben. Die Sulfhydryl-Gruppen der Proteine reagieren ebenfalls mit den ITC unter Bildung von Dithiocarbamidsaureester (Nachweis iiber die Schwefelkohlenstoff-Freisetzung aus diesen Estern). Infolge dieser Reaktionen wird in Abhangigkeit von Art und Menge des eingesetzten Isothiocyanates die pH-abhangige Proteinloslichkeit herabgesetzt, wobei gleichzeitig eine Verschiebung des isoelektrischen Bereiches in Richtung niedrigerer pH-Werte erfolgt. Die elektrophile Reaktion der ITC mit den Proteingruppen fiihrt weiterhin zu einer Veranderung im elektrophoretischen Verhalten (Harnstoff-und SDS-PAGE) der Proteine. Von den untersuchten Isothiocyanaten zeigt sich das Benzyl-ITC als der reaktivste Partner gegenuber Eiklarproteinen.

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Interaction of benzyl isothiocyanate with egg white proteins

Cited by 7 publications

References 8 publications

Some aspects of reactions of benzyl isothiocyanate with bovine sarcoplasmic proteins

Some aspects of reactions of benzyl isothiocyanate with bovine sarcoplasmic proteins

Reactivity and Stability of Glucosinolates and Their Breakdown Products in Foods

Interactions of isothiocyanates with egg white proteins

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