Abstract.
In this work, the use of methanesulfonic acid for protein hydrolysis is proposed for evaluation of Se-methionine in yeast, Brazil nuts, and possibly other selenium-rich biological samples. The hydrolysis was carried out by heating the sample with 4 mol L–1 acid at reflux for 8 h. Two chromatographic techniques (size-exclusion and ion-pairing) coupled with ICP-MS detection were used to compare the release of Se-methionine from proteins by enzymatic (proteinase K, protease XIV) and acid hydrolyses. A more efficient liberation of Se-methionine was observed by acid hydrolysis. For quantification, the sample extracts were introduced onto a C8 Alltima column, and the separation was achieved with a mobile phase containing 5 mmol L–1 hexanesulfonic acid in citrate buffer (pH 4.5)/methanol (95:5). The results obtained by standard addition showed 816±17 µg g–1 and 36.2±1.5 µg g–1 of selenium in the form of Se-methionine in yeast and nuts, respectively (65% and 75% of total selenium).
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Wrobel, K., Kannamkumarath, S.S., Wrobel, K. et al. Hydrolysis of proteins with methanesulfonic acid for improved HPLC-ICP-MS determination of seleno-methionine in yeast and nuts. Anal Bioanal Chem 375, 133–138 (2003). https://doi.org/10.1007/s00216-002-1648-5
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DOI: https://doi.org/10.1007/s00216-002-1648-5