High catalytic performances of Pseudomonas fluorescens lipase adsorbed on a new type of cyclodextrin-based nanosponges
High catalytic performances of Pseudomonas fluorescens lipase adsorbed on a new type of cyclodextrin-based nanosponges
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DOI：
10.1016/j.molcatb.2009.10.002
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发表时间：
2010-02-01
影响因子：
--
通讯作者：
Ghibaudi, Elena
中科院分区：
文献类型：
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作者：
Boscolo, Barbara;Trotta, Francesco;Ghibaudi, Elena
脂肪酶是催化三酰甘油水解（在水介质中）或酯交换反应（在微水介质中）的水溶性酶，并且涉及许多工业应用。由于界面活化的需要代表了脂肪酶应用的限制，因此一直在寻找能够满足这一要求的合适的固体支持物。在目前的工作中。我们报告了通过在新合成的基于环糊精的碳酸盐纳米海绵（CD-NS-1:4）上吸附荧光假单胞菌脂肪酶而获得的系统的初步表征。通过检查温度、pH 变化和有机溶剂（甲醇）对酶结构和功能的影响，评估了吸附在这种新型载体上的脂肪酶的活性和结构稳定性，并将其与溶液中的游离酶进行比较。我们的数据表明 Ps 的非共价相互作用。荧光脂肪酶与CD-NS-1:4导致酶结构和功能稳定，因为在类似于18摄氏度的T温下孵育66天后它仍然具有活性。还观察到相对于T、pH和有机溶剂的存在的稳定性。与溶解的酶不同，吸附的脂肪酶在 T > 40 摄氏度、pH 5 以及与 70% (v/v) 甲醇一起孵育 24 小时后具有活性（13% 残余活性）。 (C) 2009 Elsevier B.V. 保留所有权利。
Lipases are water-soluble enzymes that catalyze the hydrolysis of triacylglycerols (in aqueous media) or trans-esterification reactions (ill microaqueous media) and are involved ill a number of industrial applications. As a limit to lipase application is represented by the need for interfacial activation, the search for Suitable solid Supports able to fulfill this requirement is always ongoing. In the present work. we report the preliminary characterization of a system obtained by adsorbing Pseudomonas fluorescens lipase on a newly synthesized cyclodextrin-based carbonate nanosponge (CD-NS-1:4). The activity and structural stability of lipase adsorbed on this new support were evaluated by checking the effect of temperature, pH changes and organic solvents (methanol) on the enzyme structure and function, which were compared with those of the free enzyme in Solution. our data show that the non-covalent interaction of Ps. fluorescens lipase with CD-NS-1 :4 results in enzyme Structural and functional stabilization, as it was still active after 66 days of incubation at T similar to 18 degrees C. Stabilization with respect to T, pH and the presence of organic solvent was observed as well as. unlike the solubilized enzyme, the adsorbed lipase was active at T > 40 degrees C, at pH 5 and after 24-h incubation with 70% (v/v) methanol (13% residual activity). (C) 2009 Elsevier B.V. All rights reserved.