• Chemistry, Medicine
  • Published in
    Journal of agricultural and…
    2004
  • DOI:10.1021/jf049388y

Heat-induced redistribution of disulfide bonds in milk proteins. 1. Bovine beta-lactoglobulin.

@article{Creamer2004HeatinducedRO,
  title={Heat-induced redistribution of disulfide bonds in milk proteins. 1. Bovine beta-lactoglobulin.},
  author={Lawrence K. Creamer and Annie Bienvenue and Hanna Nilsson and Marie Paulsson and Miriam van Wanroij and Edwin K. Lowe and Skelte G. Anema and Michael J. Boland and Rafael Jim{\'e}nez-Flores},
  journal={Journal of agricultural and food chemistry},
  year={2004},
  volume={52 25},
  pages={
          7660-8
        }
}
Changes in the structure and chemistry of beta-lactoglobulin (beta-LG) play an important role in the processing and functionality of milk products. In model beta-LG systems, there is evidence that the aggregates of heated beta-LG are held together by a mixture of intermolecular non-covalent association and heat-induced non-native disulfide bonds. Although a number of non-native disulfide bonds have been identified, little is known about the initial inter- and intramolecular disulfide bond… CONTINUE READING

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Hydrolysis of â - lactoglobulin A , B and C with trypsin

  • H. Nilsson
  • 2000