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oai:ir.kagoshima-u.ac.jp:00003802 2026-03-03T16:20:19Z 70:71

Improvement of Functional Properties of Bovine Serum Albumin through Phosphorylation by Dry-Heating in the Presence of Pyrophosphate Enomoto, Hirofumi Li, Can-Peng Morizane, Kentaro Ibrahim, Hisham Sugimoto, Yasushi Ohki, Shinichi Ohtomo, Hideko Aoki, Takayoshi open access bovine serum albumin phosphorylation dry-heating structural properties functional properties 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. Blackwell 2008 eng journal article AM http://hdl.handle.net/10232/4017 https://ir.kagoshima-u.ac.jp/records/3802 18298721 https://doi.org/10.1111/j.1750-3841.2007.00634.x 00221147 AA00698289 Journal of food science 73 2 84 91 https://ir.kagoshima-u.ac.jp/record/3802/files/Main_body for review.pdf application/pdf 145.4 kB 2016-10-27 2008-03-01 https://ir.kagoshima-u.ac.jp/record/3802/files/Table 1 for review.pdf application/pdf 20.4 kB 2016-10-27 2008-03-01 https://ir.kagoshima-u.ac.jp/record/3802/files/Table 2 for review.pdf application/pdf 20.0 kB 2016-10-27 2008-03-01 https://ir.kagoshima-u.ac.jp/record/3802/files/Table 3 for review.pdf application/pdf 21.0 kB 2016-10-27 2008-03-01 https://ir.kagoshima-u.ac.jp/record/3802/files/Figure 1 for review.pdf application/pdf 124.7 kB 2016-10-27 2008-03-01 https://ir.kagoshima-u.ac.jp/record/3802/files/Figure 2 for review.pdf application/pdf 62.2 kB 2016-10-27 2008-03-01 https://ir.kagoshima-u.ac.jp/record/3802/files/Figure 3 for review.pdf application/pdf 77.6 kB 2016-10-27 2008-03-01 https://ir.kagoshima-u.ac.jp/record/3802/files/Figure 4 for review.pdf application/pdf 67.7 kB 2016-10-27 2008-03-01 https://ir.kagoshima-u.ac.jp/record/3802/files/Figure 5 for review.pdf application/pdf 62.7 kB 2016-10-27 2008-03-01 https://ir.kagoshima-u.ac.jp/record/3802/files/Figure 6 for review.pdf application/pdf 85.7 kB 2016-10-27 2008-03-01 https://ir.kagoshima-u.ac.jp/record/3802/files/Figure 7 for review.pdf application/pdf 42.7 kB 2016-10-27 2008-03-01 https://ir.kagoshima-u.ac.jp/record/3802/files/Figure 8 for review.pdf application/pdf 39.4 kB 2016-10-27 2008-03-01