TY - JOUR
T1 - Peptide composition and dipeptidyl peptidase IV inhibitory properties of β-lactoglobulin hydrolysates having similar extents of hydrolysis while generated using different enzyme-to-substrate ratios
AU - Le Maux, Solène
AU - Nongonierma, Alice B.
AU - FitzGerald, Richard J.
N1 - Publisher Copyright:
© 2017
PY - 2017/9
Y1 - 2017/9
N2 - β-Lactoglobulin hydrolysates (βlgHs) were generated using elastase at enzyme-to-substrate ratios (E:S) of 0.5, 1.0 and 1.5% in order to reach target degree of hydrolysis (DH) values of 9 and 13%. The impact of different E:S during manufacture on hydrolysates having similar DHs was assessed. Samples with similar DHs generated with different E:S showed comparable molecular mass distribution profiles and in vitro dipeptidyl peptidase IV (DPP-IV) inhibitory activities (p > 0.05). Liquid-chromatography tandem mass spectrometry (LC-MS/MS) analysis showed that 62 and 84% of the peptides identified were common within hydrolysates having a similar DH of 9 or 13%, respectively. Differences in the peptides identified within hydrolysates having similar DHs may be due to E:S dependent modifications in specificity and enzyme kinetics. Overall, this study showed that reduction in E:S while targeting the development of a similar DH for βlgHs may be employed to reduce the cost of hydrolysate production without having an adverse impact on the bioactivity and physicochemical properties studied herein.
AB - β-Lactoglobulin hydrolysates (βlgHs) were generated using elastase at enzyme-to-substrate ratios (E:S) of 0.5, 1.0 and 1.5% in order to reach target degree of hydrolysis (DH) values of 9 and 13%. The impact of different E:S during manufacture on hydrolysates having similar DHs was assessed. Samples with similar DHs generated with different E:S showed comparable molecular mass distribution profiles and in vitro dipeptidyl peptidase IV (DPP-IV) inhibitory activities (p > 0.05). Liquid-chromatography tandem mass spectrometry (LC-MS/MS) analysis showed that 62 and 84% of the peptides identified were common within hydrolysates having a similar DH of 9 or 13%, respectively. Differences in the peptides identified within hydrolysates having similar DHs may be due to E:S dependent modifications in specificity and enzyme kinetics. Overall, this study showed that reduction in E:S while targeting the development of a similar DH for βlgHs may be employed to reduce the cost of hydrolysate production without having an adverse impact on the bioactivity and physicochemical properties studied herein.
KW - Degree of hydrolysis
KW - DPP-IV inhibition
KW - Elastase
KW - Enzyme-to-substrate ratio
KW - Peptide identification
KW - β-Lactoglobulin
UR - http://www.scopus.com/inward/record.url?scp=85019562771&partnerID=8YFLogxK
U2 - 10.1016/j.foodres.2017.05.012
DO - 10.1016/j.foodres.2017.05.012
M3 - Article
C2 - 28784550
AN - SCOPUS:85019562771
SN - 0963-9969
VL - 99
SP - 84
EP - 90
JO - Food Research International
JF - Food Research International
ER -