首页> 外国专利> In the presence of active and stable organic solvents in detergent, the preparation, purification and biochemical characteristics of a novel acid and heat-resistant SPPs protease serine produced by tolerant pleurisy strain ctm10057 were studied.

In the presence of active and stable organic solvents in detergent, the preparation, purification and biochemical characteristics of a novel acid and heat-resistant SPPs protease serine produced by tolerant pleurisy strain ctm10057 were studied.

机译:在洗涤剂中存在活性和稳定的有机溶剂的情况下,研究了由耐受性胸膜炎菌株ctm10057产生的新型耐酸和耐热SPPs蛋白酶丝氨酸的制备,纯化和生化特性。

摘要

The present invention relates to uniform purification and biochemical and molecular characteristics of alkaline serine protease produced by strain ctm10057 of sajor caju. The molecular weight of the purified enzyme was estimated to be 65 000 to 10% per SDS PAGE. The sequencing of NH2 terminal also confirmed the purity of the enzyme. He showed a cherryDo not be homogenous with fungal serine protease. The optimal protease activity was obtained at pH 9.5 and 70 ° C. SPPs was completely inhibited by PMSF and DFP D. SPPs belongs to serine protease family. The range of pH (- 6-12) and high temperature (- 80-100 ℃) is very wide. Its thermal sensitivity and thermal stability are considered to be abl.Improved from 2 mM calcium The serine protease can be used as a biological additive in detergent preparation. In the presence of organic solvents (50% v / / V), especially chloroform, it is a stable peptide synthesis candidate. In the presence of SDS surfactant, SPPs enzyme also had significant stability.Surfactants (Tween 20, Tween 80 and Triton X-100)2.(Perborate de sodio et h lt sub gt 2 lt;/ In addition, SPS protease was added to detergent solution to improve the performance of dixan detergent to improve the bleaching of blood pollutants. In addition, the specificity of SPPs is that it has a wide range of specificity for protein matrix, and compared with commercial protease, it has better catalytic efficiency: pyrolytic protein X type and flavuric acid 500 L. in addition, the SPPs gene encoding SPS protease was cloned,The sequence and expression of recombinant protein (RSPS) expressed in extracellular space in E. coli BL21 plys s had the same characteristics as native protein (SPS). Therefore, SPPs protease seems to satisfy most of the good proteases that provide the synthesis of PID and biological additives in liquid and solid detergent formulations that are stable under industrial conditions.
机译:本发明涉及由大枣的ctm10057菌株产生的碱性丝氨酸蛋白酶的均匀纯化以及生化和分子特性。每个SDS PAGE估计纯化的酶的分子量为65 000至10%。 NH 2末端的测序也证实了酶的纯度。他显示出樱桃与真菌丝氨酸蛋白酶不均一。最佳蛋白酶活性在pH 9.5和70°C下获得。SPP被PMSF和DFP D完全抑制。SPP属于丝氨酸蛋白酶家族。 pH(-6-12)和高温(-80-100℃)的范围非常宽。它的热敏性和热稳定性被认为是无毒的。从2 mM钙中得到改善。丝氨酸蛋白酶可用作洗涤剂制备中的生物添加剂。在有机溶剂(50%v / / V),特别是氯仿的存在下,它是稳定的肽合成候选物。在SDS表面活性剂的存在下,SPPs酶也具有显着的稳定性。表面活性剂(吐温20,吐温80和Triton X-100)2。(过硼酸盐等)2。去污剂溶液改善了迪克森去污剂的性能,改善了血液污染物的漂白。另外,SPPs的特异性在于它对蛋白质基质具有广泛的特异性,并且与商业蛋白酶相比,具有更好的催化效率:热解蛋白X型和黄酮酸500L。此外,SPPs编码SPS的基因克隆蛋白酶,大肠杆菌BL21 plys在细胞外空间表达的重组蛋白(RSPS)的序列和表达具有与天然蛋白(SPS)相同的特征。因此,SPPs蛋白酶似乎满足大多数良好的蛋白酶的要求,它们可以在工业条件下稳定的液体和固体洗涤剂配方中提供PID和生物添加剂的合成。

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