Improvement of Functional Properties of Egg White Protein through Glycation and Phosphorylation by Dry-heating
Improvement of Functional Properties of Egg White Protein through Glycation and Phosphorylation by Dry-heating
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DOI：
10.5713/ajas.2009.80363
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发表时间：
2009-04-01
期刊：
影响因子：
--
通讯作者：
Aoki, Takayoshi
中科院分区：
文献类型：
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作者：
Enomoto, Hirofumi;Nagae, Shiho;Aoki, Takayoshi
蛋清蛋白(EWP)通过美拉德反应与麦芽五糖(MP)发生糖基化反应，然后在焦磷酸盐存在下于85℃、H4.0条件下干热1d。在相同的条件下，比较了糖化、磷酸化的EWP与天然EWP和在焦磷酸盐存在下干热磷酸化的EWP的功能特性。通过磷酸化，EWP的磷含量可提高到接近0.60%；通过与MP糖基化和随后的磷酸化，EWP的磷含量可提高到接近0.74%。通过磷酸化，EWP的凝胶迁移率增加。单独的磷酸化和糖基化后的进一步磷酸化可显著提高EWP在pH 7.0条件下的抗热不溶性稳定性。糖基化和磷酸化显著降低抗卵清蛋白抗体应答，糖基化后进一步磷酸化则进一步降低。糖基化、磷酸化和糖基化后的磷酸化可显著降低抗卵粘液抗体的应答。两种磷酸化方法均提高了EWP的钙磷溶解能力。
Egg white protein (EWP) was glycated with maltopentaose (MP) through the Maillard reaction and subsequently phosphorylated by 85 degrees C dry-heating at H 4.0 for 1 d in the presence of pyrophosphate. The functional properties of glycated, phosphorylated EWP were compared with those of native EWP and with EWP which was phosphorylated by dry-heating in the presence of pyrophosphate under the same conditions. The phosphorus content of EWP was increased to similar to 0.60% by phosphorylation, and to similar to 0.74% by glycation with MP and subsequent phosphorylation. The electrophoretic mobility of EWP increased through phosphorylation. The stability of EWP against heat-induced insolubility at pH 7.0 was considerably improved by phosphorylation alone and further by phosphorylation after glycation. The anti-ovalbumin antibody response was reduced significantly by glycation and phosphorylation, and further reduced by phosphorylation after glycation. The anti-ovomucoid antibody response was reduced significantly by glycation, phosphorylation and phosphorylation after glycation. The calcium phosphate-solubilizing ability of EWP was enhanced by both phosphorylation methods.