Proteomic characterisation of heat-induced hydrolysis of sodium caseinate

McGrath, Brian A. and Kinsella, Michael and Huppertz, Thom and McSweeney, Paul L.H. and Kelly, Alan L. (2016) Proteomic characterisation of heat-induced hydrolysis of sodium caseinate. International Dairy Journal, 53. pp. 51-59. ISSN 0958-6946

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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.

Item Type: Article
Additional Information: 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.
Uncontrolled Keywords: /dk/atira/pure/subjectarea/asjc/1100/1106
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Depositing User: Admin SSL
Date Deposited: 19 Oct 2022 23:08
Last Modified: 26 Jun 2023 03:00

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