Enzymatic cross-linking of proteins with tyrosinase

被引:103
作者
Thalmann, CR [1 ]
Lötzbeyer, T [1 ]
机构
[1] Bremerhavener Inst Lebensmitteltechnol & Bioverfa, D-27572 Bremerhaven, Germany
关键词
protein cross-linking; tyrosinase; whey protein; alpha-lactalbumin; beta-lactoglobulin;
D O I
10.1007/s00217-001-0455-0
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Tyrosinase (EC 1.14.18.1), usually known as the enzyme responsible for the enzymatic browning of fruits and vegetables, has been demonstrated to induce cross-linking of the whey proteins alpha-lactalbumin and beta-lactoglobulin. The maximum degree of polymerisation for 1.5 mg/ml protein has been achieved at a tyrosinase activity of about 330 U/ml in the presence of a 2 mM concentration of caffeic acid. The pH optimum for the cross-linking reaction was detected at pH 4-5 for alpha-lactalbumin and beta-lactoglobulin, in contrast to pH 7 for lysozyme, a non-whey protein, indicating that for the whey proteins the initial enzymatic oxidation of the phenolic compound is not the rate limiting step for the reaction. In contrast to beta-lactoglobulin and lysozyme, for alpha-lactalbumin a direct cross-linking even without addition of caffeic acid has been proved. In this manner alpha-lactalbumin polymers with a molecular weight larger than 300 kDa have been produced by increasing the reaction temperature up to 50 degreesC. The results of the present study represent a basis for the creation of new high molecular weight proteins. Due to a different reaction mechanism and different points of linkage, tyrosinase-induced protein cross-linking may be a promising alternative to the already established use of transglutaminase for food application.
引用
收藏
页码:276 / 281
页数:6
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