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首页> 外文期刊>Journal of industrial microbiology & biotechnology >Immobilization in the presence of Triton X-100: modifications in activity and thermostability of Geobacillus thermoleovorans CCR11 lipase
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Immobilization in the presence of Triton X-100: modifications in activity and thermostability of Geobacillus thermoleovorans CCR11 lipase

机译：Triton X-100存在下的固定化：热地芽孢杆菌CCR11脂肪酶的活性和热稳定性的改变

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摘要

A partially purified lipase produced by the thermophile Geobacillus thermoleovorans CCR11 was immobilized by adsorption on porous polypropylene (Accurel EP-100) in the presence and absence of 0.1% Triton X-100. Lipase production was induced in a 2.5% high oleic safflower oil medium and the enzyme was partially purified by diafiltration (co. 500,000 Da). Immobilization conditions were established at 25 degrees C, pH 6, and a protein concentration of 0.9 mg/mL in the presence and absence of 0.1% Triton X-100. Immobilization increased enzyme thermostability but there was no change in neither the optimum pH nor in pH resistance irrelevant to the presence of the detergent during immobilization. Immobilization with or without Triton X-100 allowed the reuse of the lipase preparation for 11 and 8 cycles, respectively. There was a significant difference between residual activity of immobilized and soluble enzyme after 36 days of storage at 4 degrees C (P < 0.05). With respect to chain length specificity, the immobilized lipase showed less activity over short chain esters than the soluble lipase. The immobilized lipase showed good resistance to desorption with phosphate buffer and NaCl; minor loses with detergents were observed (less than 50% with Triton X-100 and Tween-80), but activity was completely lost with SDS. Immobilization of G. thermoleovorans CCR11 lipase in porous polypropylene is a simple and easy method to obtain a biocatalyst with increased stability, improved performance, with the possibility for re-use, and therefore an interesting potential use in commercial conditions.
机译：在存在和不存在0.1％Triton X-100的情况下，通过吸附在多孔聚丙烯（Accurel EP-100）上，将嗜热嗜热芽孢杆菌CCR11产生的部分纯化的脂肪酶固定化。在2.5％高油酸红花油培养基中诱导脂肪酶的产生，并通过渗滤（co。500,000 Da）部分纯化该酶。在存在和不存在0.1％Triton X-100的条件下，将固定条件设定在25℃，pH 6和0.9 mg / mL的蛋白质浓度下。固定化增加了酶的热稳定性，但是与固定化过程中去污剂的存在无关，最佳pH和耐pH性均没有变化。在有或没有Triton X-100的情况下固定化，可使脂肪酶制剂分别重复使用11和8个循环。在4摄氏度下储存36天后，固定化酶和可溶性酶的残留活性之间存在显着差异（P <0.05）。关于链长特异性，固定化脂肪酶对短链酯的活性低于可溶性脂肪酶。固定化的脂肪酶对磷酸盐缓冲液和NaCl的解吸表现出良好的抵抗力。观察到清洁剂的少量损失（Triton X-100和Tween-80的损失少于50％），但SDS的活性完全丧失。在多孔聚丙烯中固定G.thermoleovorans CCR11脂肪酶是一种获得稳定性高，性能提高，可以重复使用的生物催化剂的简便方法，因此有可能在商业条件下使用。

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