TY - JOUR
T1 - Proteomic characterisation of heat-induced hydrolysis of sodium caseinate
AU - McGrath, Brian A.
AU - Kinsella, Michael
AU - Huppertz, Thom
AU - McSweeney, Paul L.H.
AU - Kelly, Alan L.
N1 - Funding Information:
The work described herein was supported by Enterprise Ireland under Grant Number CC20080001 . All mass spectroscopy work was conducted on a Waters Xevo G2 Quadrupole-Time-Of-Flight (Q-TOF) LC-MS instrument funded under the HEA's Programme for Research in Third-Level Institutions (PRTLI) and co-funded under the European Regional Development Fund .
Publisher Copyright:
© 2015 Elsevier Ltd.
PY - 2016/2/1
Y1 - 2016/2/1
N2 - The hydrolysis of sodium caseinate during heating for up to 120 min at pH 7.0 and 130 °C was investigated. The formation of 2% trichloroacetic acid (TCA)-soluble peptides was studied using spectrofluorimetry and high resolution liquid chromatography-mass spectrometry (LC-MS), whereas sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) was used to study hydrolysis of the caseins. LC-MS and spectrofluorimetry showed an increase in 2% TCA-soluble peptides over time, confirming that proteolysis had occurred, whereas SDS-PAGE showed a decrease in band intensity for the main caseins over time. In total, 1023 casein-derived peptides were identified. For eleven of the most abundant peptides, release and breakdown were modelled. Peptide bonds containing Pro, Ser, Asn and/or Asp were preferentially hydrolysed during heating. The production of peptides in this manner may represent a novel alternative to enzymatic hydrolysis strategies.
AB - The hydrolysis of sodium caseinate during heating for up to 120 min at pH 7.0 and 130 °C was investigated. The formation of 2% trichloroacetic acid (TCA)-soluble peptides was studied using spectrofluorimetry and high resolution liquid chromatography-mass spectrometry (LC-MS), whereas sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) was used to study hydrolysis of the caseins. LC-MS and spectrofluorimetry showed an increase in 2% TCA-soluble peptides over time, confirming that proteolysis had occurred, whereas SDS-PAGE showed a decrease in band intensity for the main caseins over time. In total, 1023 casein-derived peptides were identified. For eleven of the most abundant peptides, release and breakdown were modelled. Peptide bonds containing Pro, Ser, Asn and/or Asp were preferentially hydrolysed during heating. The production of peptides in this manner may represent a novel alternative to enzymatic hydrolysis strategies.
UR - http://www.scopus.com/inward/record.url?scp=84946782072&partnerID=8YFLogxK
U2 - 10.1016/j.idairyj.2015.09.006
DO - 10.1016/j.idairyj.2015.09.006
M3 - Article
AN - SCOPUS:84946782072
VL - 53
SP - 51
EP - 59
JO - International Dairy Journal
JF - International Dairy Journal
SN - 0958-6946
ER -