Characterization of an invertase with pH tolerance and truncation of its N-terminal to shift optimum activity toward neutral pH.
Characterization of an invertase with pH tolerance and truncation of its N-terminal to shift optimum activity toward neutral pH.
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具有 pH 耐受性的蔗糖酶的表征及其 N 末端的截断，以将最佳活性转向中性 pH
DOI：
10.1371/journal.pone.0062306
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发表时间：
2013
期刊：
影响因子：
3.7
通讯作者：
Huang R
中科院分区：
文献类型：
--
作者：
Du L;Pang H;Wang Z;Lu J;Wei Y;Huang R
迄今为止鉴定出的大多数转化酶在酸性pH值下具有最佳活性，并且不耐受中性或碱性环境。在此，描述了一种名为uninv2的酸性转化酶。Uninv2包含586个氨基酸，具有一个100个氨基酸的N末端结构域、一个催化结构域和一个C末端结构域。以蔗糖为底物，uninv2的活性在pH值为4.5和45°C时最佳。去除uninv2的N末端结构域使最适pH值变为6.0，同时其最适温度仍保持在45°C。uninv2和截短的酶在37°C的中性pH值下都保持高度稳定，并且在4°C的最适pH值下稳定长达30天。这些特性使它们远远优于主要用作工业酶的酿酒酵母转化酶。
Most invertases identified to date have optimal activity at acidic pH, and are intolerant to neutral or alkaline environments. Here, an acid invertase named uninv2 is described. Uninv2 contained 586 amino acids, with a 100 amino acids N-terminal domain, a catalytic domain and a C-terminal domain. With sucrose as the substrate, uninv2 activity was optimal at pH 4.5 and at 45°C. Removal of N-terminal domain of uninv2 has shifted the optimum pH to 6.0 while retaining its optimum temperaure at 45°C. Both uninv2 and the truncated enzyme retained highly stable at neutral pH at 37°C, and they were stable at their optimum pH at 4°C for as long as 30 days. These characteristics make them far superior to invertase from Saccharomyces cerevisiae, which is mostly used as industrial enzyme.
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