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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Functional improvement of beta-lactoglobulin by conjugating with alginate lyase-lysate.
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Functional improvement of beta-lactoglobulin by conjugating with alginate lyase-lysate.

机译：通过与藻酸盐裂解酶裂解物结合来改善β-乳球蛋白的功能。

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摘要

Bovine beta-lactoglobulin-alginic acid oligosaccharide (beta-LG-ALGO) conjugate was prepared by the Maillard reaction to improve the function of beta-LG. The molar ratio of beta-LG:ALGO in the conjugate was 1:7. Its isoelectric point was 4.55, whichwas lower than that of beta-LG. Fluorescence studies suggested that the conformation around Trp had changed in the conjugate and that its surface was covered with saccharide chains. Structural analyses with monoclonal antibodies indicated that the conformation around Val15-Ile29 (beta-sheet) in the conjugate had changed, while native structure was maintained around Thr125-Lys135 (alpha-helix). By conjugation with ALGO, beta-LG had high heat stability. The emulsifying activity and the aggregating properties of beta-LG were improved in the conjugate.
机译：通过美拉德反应制备了牛β-乳球蛋白-藻酸寡糖（β-LG-ALGO）结合物，以改善β-LG的功能。共轭物中β-LG：ALGO的摩尔比为1：7。等电点为4.55，低于β-LG。荧光研究表明，缀合物中Trp周围的构象发生了变化，其表面被糖链覆盖。用单克隆抗体进行的结构分析表明，缀合物中Val15-Ile29（β-折叠）周围的构象发生了变化，而Thr125-Lys135（α-螺旋）周围的天然结构得以保持。通过与ALGO结合，β-LG具有很高的热稳定性。结合物中β-LG的乳化活性和聚集性质得到改善。

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