REDESIGNING A SWEET PROTEIN - INCREASED STABILITY AND RENATURABILITY
REDESIGNING A SWEET PROTEIN - INCREASED STABILITY AND RENATURABILITY
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DOI：
10.1093/protein/2.8.571
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发表时间：
1989-08-01
期刊：
影响因子：
--
通讯作者：
LEE, TK
中科院分区：
文献类型：
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作者：
KIM, SH;KANG, CH;LEE, TK
Monellin是来自非洲浆果的两种天然蛋白质之一，具有很强的甜味。Monellin是两者中较小的一个，由两个肽组成。当蛋白质在酸性pH下加热到50℃以上时，就会失去甜味。基于Monellin的晶体结构，我们使用从同一分子复制并移植的几个不同的连接子将这两条链融合成一条单链。其中一种新设计的蛋白质和天然蛋白质一样甜，在温度或pH变化时更稳定，即使在低pH值下加热到100℃后也很容易复性。
Monellin is one of two natural proteins from African berries with potent sweet taste. Monellin is the smaller of the two, and consists of two peptides. The protein loses sweetness when heated above 50.degree.C under acidic pH. Based on the crystal structure of monellin we have fused the two chains into a single chain using several different linkers copied and ''transplanted'' from the same molecule. One of the newly designed proteins is as potently sweet as the natural one, is more stable upon temperature or pH changes, and renatures easily even after heating to 100.degree.C at low pH.