Phosphopantetheinyl transferases are of tremendous enthusiasm inferable from their fundamental parts in activating polyketide, fatty acid, and non-ribosomal peptide synthetase enzymes and additionally an increasing number of biotechnological applications. The present study reports the identification of sfp gene from the Paenibacillus sp. D9, which encompasses 693 bp encoding a 230-amino acid protein with a molecular weight of 25.3 kDa. The amino acid sequence Paenibacillus sp. D9 Sfp revealed more than 90% sequence identity to other Sfp proteins from other Paenibacillus. The sfp gene was cloned and recovered efficiently using affinity chromatography with maximal specific phosphopantetheinyl transferase activity at an optimal pH of 8.0 and temperature of 30 °C. The enzyme also exhibited stability under a wide-ranging pH and temperature. The presence of Zn2+, Cu2+, and Fe2+ ions improved the enzymatic activity, while other metals such as Ni2+, Co2+, and Mg2+ had inhibitory effects. The introduction of EDTA also displayed no inhibition. Kinetic parameters were obtained having values of 4.52 mg/mL, 35.33 U/mg, 3.64 s-1, and 0.104 mM-1 s-1 for Km, Vmax, kcat, and kcat/Km, respectively. The biosurfactant synthesized by the recombinant BioSp was found to be surface active, reducing the surface tension to 33.7 mN/m on the glucose substrate after 5 days of incubation at 37 °C. The recombinant Escherichia coli strain also exhibited an improvement in biosurfactant yield (1.11 g/L) when contrasted with 0.52 g/L from Paenibacillus sp. D9. High esterase activity of 2.55 IU/mL using p-nitrophenyl acetate was observed on the recombinant strain, as the protein connected with the release of the biosurfactant was observed to be an esterase. The characteristics of improved biosurfactant and esterase synthesis by hyper-producing recombinant strain possess numerous values from biotechnology standpoint.

中文翻译：

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在脂肽生物表面活性剂的生物合成中，Sfp型磷酸泛亚锡基转移酶的异源表达是必不可少的。

从其在活化聚酮化合物，脂肪酸和非核糖体肽合成酶中的基本组成部分以及其他越来越多的生物技术应用中可以推断出，磷酸泛肽基转移酶具有极大的热情。本研究报告从Paenibacillus sp。鉴定sfp基因。D9，其包含693 bp，编码分子量为25.3 kDa的230个氨基酸的蛋白质。氨基酸序列Paenibacillus sp。D9 Sfp与来自其他Paenibacillus的其他Sfp蛋白的序列同一性超过90％。sfp基因被克隆并使用亲和色谱法进行了有效的回收，在最佳pH值为8.0且温度为30°C的条件下，磷酸泛肽亚基转移酶的活性最高。该酶在宽范围的pH和温度下也表现出稳定性。Zn2 +，Cu2 +和Fe2 +离子的存在改善了酶的活性，而其他金属如Ni2 +，Co2 +和Mg2 +则具有抑制作用。EDTA的引入也没有显示出抑制作用。获得的动力学参数的Km，Vmax，kcat和kcat / Km值分别为4.52 mg / mL，35.33 U / mg，3.64 s-1和0.104 mM-1 s-1。发现由重组BioSp合成的生物表面活性剂具有表面活性，在37°C下孵育5天后，其在葡萄糖底物上的表面张力降低至33.7 mN / m。与来自Paenibacillus sp。的0.52 g / L相比，重组大肠杆菌菌株还显示出生物表面活性剂产量的提高（1.11 g / L）。D9。在重组菌株上观察到使用对硝基苯乙酸酯的高酯酶活性为2.55 IU / mL，因为观察到与生物表面活性剂释放有关的蛋白质是酯酶。从生物技术的观点来看，通过高产重组菌株改进的生物表面活性剂和酯酶合成的特征具有许多价值。