TY - JOUR
T1 - Quantitative mass spectrometric analysis of dipeptides in protein hydrolysate by a TNBS derivatization-aided standard addition method
AU - Hanh, Vu Thi
AU - Kobayashi, Yutaro
AU - Maebuchi, Motohiro
AU - Nakamori, Toshihiro
AU - Tanaka, Mitsuru
AU - Matsui, Toshiro
N1 - Publisher Copyright:
© 2015 Elsevier Ltd. All rights reserved.
PY - 2016/6/3
Y1 - 2016/6/3
N2 - The aim of this study was to establish, through a standard addition method, a convenient quantification assay for dipeptides (GY, YG, SY, YS, and IY) in soybean hydrolysate using 2,4,6-trinitrobenzene sulfonate (TNBS) derivatization-aided LC-TOF-MS. Soybean hydrolysate samples (25.0 mg mL-1) spiked with target standards were subjected to TNBS derivatization. Under the optimal LC-MS conditions, five target dipeptides derivatized with TNBS were successfully detected. Examination of the standard addition curves, with a correlation coefficient of r2 > 0.979, provided a reliable quantification of the target dipeptides, GY, YG, SY, YS, and IY, in soybean hydrolysate to be 424 ± 20, 184 ± 9, 2188 ± 199, 327 ± 16, and 2211 ± 133 μg g-1 of hydrolysate, respectively. The proposed LC-MS assay is a reliable and convenient assay method, with no interference from matrix effects in hydrolysate, and with no requirement for the use of an isotope labeled internal standard.
AB - The aim of this study was to establish, through a standard addition method, a convenient quantification assay for dipeptides (GY, YG, SY, YS, and IY) in soybean hydrolysate using 2,4,6-trinitrobenzene sulfonate (TNBS) derivatization-aided LC-TOF-MS. Soybean hydrolysate samples (25.0 mg mL-1) spiked with target standards were subjected to TNBS derivatization. Under the optimal LC-MS conditions, five target dipeptides derivatized with TNBS were successfully detected. Examination of the standard addition curves, with a correlation coefficient of r2 > 0.979, provided a reliable quantification of the target dipeptides, GY, YG, SY, YS, and IY, in soybean hydrolysate to be 424 ± 20, 184 ± 9, 2188 ± 199, 327 ± 16, and 2211 ± 133 μg g-1 of hydrolysate, respectively. The proposed LC-MS assay is a reliable and convenient assay method, with no interference from matrix effects in hydrolysate, and with no requirement for the use of an isotope labeled internal standard.
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U2 - 10.1016/j.foodchem.2015.05.053
DO - 10.1016/j.foodchem.2015.05.053
M3 - Article
C2 - 26212980
AN - SCOPUS:84930637511
SN - 0308-8146
VL - 190
SP - 345
EP - 350
JO - Food Chemistry
JF - Food Chemistry
ER -