Ine Rombouts

Summary

Affiliation: Katholieke Universiteit Leuven
Country: Belgium

Publications

  1. doi request reprint Identification of lanthionine and lysinoalanine in heat-treated wheat gliadin and bovine serum albumin using tandem mass spectrometry with higher-energy collisional dissociation
    Ine Rombouts
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre LFoRCe, KU Leuven, Kasteelpark Arenberg 20, Box 2463, 3001, Leuven, Belgium
    Amino Acids 48:959-71. 2016
  2. pmc Improved identification of wheat gluten proteins through alkylation of cysteine residues and peptide-based mass spectrometry
    Ine Rombouts
    German Research Center for Food Chemistry, Leibniz Institute, Lise Meitner Strasse 34, D 85354 Freising, Germany
    Sci Rep 3:2279. 2013
  3. doi request reprint Cross-linking of wheat gluten proteins during production of hard pretzels
    Ine Rombouts
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre LFoRCe, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, P O Box 2463, 3001, Heverlee, Belgium
    Amino Acids 42:2429-38. 2012
  4. doi request reprint Wheat gluten amino acid composition analysis by high-performance anion-exchange chromatography with integrated pulsed amperometric detection
    Ine Rombouts
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Center, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, B 3001 Leuven, Belgium
    J Chromatogr A 1216:5557-62. 2009
  5. doi request reprint Identification of isopeptide bonds in heat-treated wheat gluten peptides
    Ine Rombouts
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre LFoRCe, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, Box 2463, B 3001 Leuven, Belgium
    J Agric Food Chem 59:1236-43. 2011
  6. doi request reprint Wheat gluten amino acid analysis by high-performance anion-exchange chromatography with integrated pulsed amperometric detection
    Ine Rombouts
    Laboratory of Food Chemistry and Biochemistry, Leuven Food Science and Nutrition Research Centre LFoRCe, Katholieke Universiteit Leuven, Leuven, Belgium
    Methods Mol Biol 828:329-37. 2012
  7. doi request reprint Heat-induced cross-linking and degradation of wheat gluten, serum albumin, and mixtures thereof
    Ine Rombouts
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre LFoRCe, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, B 3001 Leuven, Belgium
    J Agric Food Chem 60:10133-40. 2012
  8. doi request reprint The kinetics of β-elimination of cystine and the formation of lanthionine in gliadin
    Bert Lagrain
    Centre for Food and Microbial Technology and Leuven Food Science and Nutrition Research Centre, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, B 3001 Leuven, Belgium
    J Agric Food Chem 58:10761-7. 2010
  9. pmc Identification of intact high molecular weight glutenin subunits from the wheat proteome using combined liquid chromatography-electrospray ionization mass spectrometry
    Bert Lagrain
    German Research Center for Food Chemistry, Freising, Germany
    PLoS ONE 8:e58682. 2013
  10. doi request reprint Kinetics of heat-induced polymerization of gliadin
    Bert Lagrain
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre LFoRCe, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, B 3001 Leuven, Belgium
    J Agric Food Chem 59:2034-9. 2011

Collaborators

Detail Information

Publications17

  1. doi request reprint Identification of lanthionine and lysinoalanine in heat-treated wheat gliadin and bovine serum albumin using tandem mass spectrometry with higher-energy collisional dissociation
    Ine Rombouts
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre LFoRCe, KU Leuven, Kasteelpark Arenberg 20, Box 2463, 3001, Leuven, Belgium
    Amino Acids 48:959-71. 2016
    ..The detection of inter-chain lanthionine in both bovine serum albumin and wheat gliadin suggests the significance of these cross-links for food texture...
  2. pmc Improved identification of wheat gluten proteins through alkylation of cysteine residues and peptide-based mass spectrometry
    Ine Rombouts
    German Research Center for Food Chemistry, Leibniz Institute, Lise Meitner Strasse 34, D 85354 Freising, Germany
    Sci Rep 3:2279. 2013
    ..However, more peptides were detected after labeling gluten proteins with 4-VP and IDAM than with ICAT...
  3. doi request reprint Cross-linking of wheat gluten proteins during production of hard pretzels
    Ine Rombouts
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre LFoRCe, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, P O Box 2463, 3001, Heverlee, Belgium
    Amino Acids 42:2429-38. 2012
    ..No indications for Maillard-derived cross-links or LAL in pretzel dough immediately after dipping were found, even when severe dipping conditions were used...
  4. doi request reprint Wheat gluten amino acid composition analysis by high-performance anion-exchange chromatography with integrated pulsed amperometric detection
    Ine Rombouts
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Center, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, B 3001 Leuven, Belgium
    J Chromatogr A 1216:5557-62. 2009
    ..Results for the other amino acids obtained by the different methods were linearly correlated (r>0.99, slope=1.03)...
  5. doi request reprint Identification of isopeptide bonds in heat-treated wheat gluten peptides
    Ine Rombouts
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre LFoRCe, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, Box 2463, B 3001 Leuven, Belgium
    J Agric Food Chem 59:1236-43. 2011
    ..Heating HMW-GS lysine- and glutamine-containing peptides induced the formation of isopeptide bonds, thereby supporting the above hypothesis. The level of isopeptide bond formation increased with heating time...
  6. doi request reprint Wheat gluten amino acid analysis by high-performance anion-exchange chromatography with integrated pulsed amperometric detection
    Ine Rombouts
    Laboratory of Food Chemistry and Biochemistry, Leuven Food Science and Nutrition Research Centre LFoRCe, Katholieke Universiteit Leuven, Leuven, Belgium
    Methods Mol Biol 828:329-37. 2012
    ..Gradient conditions including an extra eluent allow multiple sequential sample analyses without risk of Glu accumulation on the anion-exchange column which otherwise would result from high Gln levels in gluten proteins...
  7. doi request reprint Heat-induced cross-linking and degradation of wheat gluten, serum albumin, and mixtures thereof
    Ine Rombouts
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre LFoRCe, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, B 3001 Leuven, Belgium
    J Agric Food Chem 60:10133-40. 2012
    ..In addition, above 110 °C, β-elimination of cystine led to non-SS cross-links. Intramolecular SS bonds more often transformed in intermolecular non-SS bonds in BSA than in gluten. ..
  8. doi request reprint The kinetics of β-elimination of cystine and the formation of lanthionine in gliadin
    Bert Lagrain
    Centre for Food and Microbial Technology and Leuven Food Science and Nutrition Research Centre, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, B 3001 Leuven, Belgium
    J Agric Food Chem 58:10761-7. 2010
    ..g., bread making, but may well contribute to gluten network formation during the production of soft wheat products. It may also well be relevant in the production of bioplastics made from gluten...
  9. pmc Identification of intact high molecular weight glutenin subunits from the wheat proteome using combined liquid chromatography-electrospray ionization mass spectrometry
    Bert Lagrain
    German Research Center for Food Chemistry, Freising, Germany
    PLoS ONE 8:e58682. 2013
    ....
  10. doi request reprint Kinetics of heat-induced polymerization of gliadin
    Bert Lagrain
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre LFoRCe, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, B 3001 Leuven, Belgium
    J Agric Food Chem 59:2034-9. 2011
    ..Gliadin extractability was much less affected. Under the experimental conditions, gliadin polymerization through SH-SS interchange occurred much more rapidly than β-elimination of cystine...
  11. doi request reprint Impact of casein and egg white proteins on the structure of wheat gluten-based protein-rich food
    Arno G B Wouters
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Center LFORCE, Katholieke Universiteit Leuven, B 3001, Leuven, Belgium
    J Sci Food Agric 96:757-63. 2016
    ..This study investigated the potential of egg white and bovine milk casein with well-balanced amino acid composition to increase the quality of wheat gluten-based protein-rich foods...
  12. pmc Formation and reshuffling of disulfide bonds in bovine serum albumin demonstrated using tandem mass spectrometry with collision-induced and electron-transfer dissociation
    Ine Rombouts
    Laboratory of Food Chemistry and Biochemistry, Leuven Food Science and Nutrition Research Centre LFoRCe, KU Leuven, Kasteelpark Arenberg 20, Box 2463, B 3001 Leuven, Belgium
    Sci Rep 5:12210. 2015
    ..The here developed approach holds promise for exploring disulfide bond formation and reshuffling in various proteins under conditions relevant for chemical, biochemical, pharmaceutical and food processing...
  13. doi request reprint Impact of parboiling conditions on Maillard precursors and indicators in long-grain rice cultivars
    Lieve Lamberts
    Laboratory of Food Chemistry and Biochemistry, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, B 3001 Leuven, Belgium Electronic address
    Food Chem 110:916-22. 2008
    ..The strong correlation (r=0.89) between the free HMF levels and the increase in redness of parboiled brown rices suggested that Maillard browning was reflected more in the red than in the yellow colour. ..
  14. doi request reprint Foam fractionation as a tool to study the air-water interface structure-function relationship of wheat gluten hydrolysates
    Arno G B Wouters
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Center LFORCE, KU Leuven, Kasteelpark Arenberg 20, B 3001 Leuven, Belgium Electronic address
    Colloids Surf B Biointerfaces 151:295-303. 2016
    ..These peptides were also more concentrated in un-fractionated DH 2 hydrolysates, which had high FS, than in DH 6 hydrolysates, which had low FS. These peptides most likely play a key role in stabilizing the air-water interface...
  15. doi request reprint The Role of Wheat and Egg Constituents in the Formation of a Covalent and Non-covalent Protein Network in Fresh and Cooked Egg Noodles
    Marlies A Lambrecht
    KU Leuven, Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre LFoRCe, Kasteelpark Arenberg 20, B 3001, Leuven, Belgium
    J Food Sci 82:24-35. 2017
    ..Hydrogen bonds and covalent cross-links are probably the main determinants of the extensibility of cooked noodles...
  16. doi request reprint Prediction of heat-induced polymerization of different globular food proteins in mixtures with wheat gluten
    Marlies A Lambrecht
    KU Leuven, Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre LFoRCe, Kasteelpark Arenberg 20, B 3001 Leuven, Belgium Electronic address
    Food Chem 221:1158-1167. 2017
    ..The level of accessible free sulfhydryl groups and the surface hydrophobicity of unfolded globular proteins were the main characteristics in determining the co-protein effects in gluten mixtures...
  17. doi request reprint Impact of extraction and elution media on non-size effects in size exclusion chromatography of proteins
    Marlies A Lambrecht
    Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre LFoRCe, KU Leuven, Kasteelpark Arenberg 20, B 3001 Leuven, Belgium Electronic address
    J Chromatogr A 1415:100-7. 2015
    ..Most gluten and globular proteins are extractable in sodium phosphate buffer (0.050M; pH 6.8) containing 2.0% (w/v) SDS. This chromatographic medium allows analyzing mixtures of various proteins without any non-size effects. ..