@article{oai:ir.kagoshima-u.ac.jp:00003802,
 author = {Enomoto, Hirofumi and Li, Can-Peng and Morizane, Kentaro and Ibrahim, Hisham and Sugimoto, Yasushi and Ohki, Shinichi and Ohtomo, Hideko and Aoki, Takayoshi},
 issue = {2},
 journal = {Journal of food science},
 month = {},
 note = {Bovine serum albumin (BSA) was phosphorylated by two methods. One is dry-heating in the presence of pyrophosphate, and the other is conjugation with maltopentaose through the Maillard reaction and subsequent dry-heating in the presence of pyrophosphate. The phosphorus content of BSA was increased to ~0.45% by dry-heating at pH 4.0 and 85 °C for 5 d in the presence of pyrophosphate, and ~0.91% by glycation and subsequent phosphorylation. The circular dichroism spectra showed that the change of secondary structure in the BSA molecule by phosphorylation was mild. However, tryptophan fluorescence intensity of BSA decreased by phosphorylation. The differential scanning calorimetry thermograms of BSA showed a disappearing of the first peak and a lowering of the second peak denaturation temperature by phosphorylation. These results indicated molten (partially unfolded) conformations of BSA formed by both phosphorylation methods. The functional properties of BSA such as heat stability and calcium phosphate solubilizing ability were improved by phosphorylation alone and further by phosphorylation after glycation. Transparent gels of BSA with relatively high water-holding capacity were obtained by phosphorylation alone, and the immunogenicity of BSA was reduced significantly by glycation and phosphorylation, respectively.},
 pages = {84--91},
 title = {Improvement of Functional Properties of Bovine Serum Albumin through Phosphorylation by Dry-Heating in the Presence of Pyrophosphate},
 volume = {73},
 year = {2008}
}