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首页> 外文期刊>European food research and technology =: Zeitschrift fur Lebensmittel-Untersuchung und -Forschung. A >Purification of a novel protease enzyme from kesinai plant (Streblus asper) leaves using a surfactant-salt aqueous micellar two-phase system: a potential low cost source of enzyme and purification method.
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Purification of a novel protease enzyme from kesinai plant (Streblus asper) leaves using a surfactant-salt aqueous micellar two-phase system: a potential low cost source of enzyme and purification method.

机译：使用表面活性剂-盐水溶液胶束两相系统从Kesinai植物（Streblus asper）叶片中纯化新型蛋白酶：一种潜在的低成本酶来源和纯化方法。

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Serine protease from kesinai leaves was purified for the first time by a surfactant-polymer aqueous micellar two-phase system. The effectiveness of different types and concentrations of non-ionic surfactants (Pluronic series and X-114) on the partitioning behaviour of the protease was evaluated. The results showed that the enzyme preferentially partitioned into the bottom surfactant-rich phase, while the hydrophilic amino acid preferred the top aqueous phase. This distribution of the enzyme is due to the hydrophobic interaction of the serine protease with the hydrophobic lid of the micelle core in the bottom phase. The influence of different types of salts (K2SO4, KH2PO4, KCl and KNO3) on the purification and selectivity of the enzyme was determined. The protease partitioning in the bottom phase increased in the presence of KNO3, which confirmed that the salt was able to improve the protein solubility in bottom phase and increase the hydrophobic interaction between the two phases. In addition, the protease from the bottom phase was re-extracted to a new aqueous phase solution to remove and recycle the surfactant. Addition of potassium thiocyanate led to the partitioning of the enzyme in top aqueous phase due to high ionic strength of SCN-, which forced the lighter micellar phase toward the upper position of the system. A high purification factor (10.3) and yield of 92 % of the enzyme were achieved in a solution of 31 % of Pluronic L61 using 0.3 % KNO3 and 50 % crude feedstock at pH 7.0. copyright Springer-Verlag Berlin Heidelberg 2013.
机译：通过表面活性剂-聚合物水胶束两相系统首次纯化来自凯斯奈叶的丝氨酸蛋白酶。评估了不同类型和浓度的非离子表面活性剂（Pluronic系列和X-114）对蛋白酶分配行为的有效性。结果表明，该酶优先分配在底部富表面活性剂的相中，而亲水氨基酸则优先选择顶部水相。酶的这种分布是由于丝氨酸蛋白酶与底部相中胶束核心的疏水盖的疏水相互作用。不同类型的盐（K 2 SO 4 ，KH 2 PO 4 ，KCl和KNO < sub> 3 ）对酶的纯化和选择性进行了测定。在存在KNO 3 的情况下，底部相中的蛋白酶分配增加，这证实了该盐能够改善底部相中的蛋白质溶解性并增加两相之间的疏水相互作用。另外，将来自底部相的蛋白酶再次萃取到新的水相溶液中以去除和再循环表面活性剂。由于SCN -的高离子强度，硫氰酸钾的添加导致了酶在顶部水相中的分配，这迫使较轻的胶束相朝着系统的上部移动。在31％的Pluronic L61溶液中，使用0.3％的KNO 3 和50％的pH 7.0的粗原料，可实现高纯化因子（10.3）和92％的酶收率。版权所有Springer-Verlag Berlin Heidelberg 2013。

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