Improving catalytic performance of Burkholderia cepacia lipase immobilized on macroporous resin NKA
Improving catalytic performance of Burkholderia cepacia lipase immobilized on macroporous resin NKA
复制标题
提高大孔树脂NKA固定化洋葱伯克霍尔德氏菌脂肪酶的催化性能
DOI：
10.1016/j.molcatb.2011.03.007
复制
发表时间：
2011-08-01
影响因子：
--
通讯作者：
Yan, Yunjun
中科院分区：
文献类型：
--
作者：
Liu, Tao;Liu, Yun;Yan, Yunjun
为了提高洋葱伯克霍尔德菌脂肪酶的催化性能，采用生物印迹和界面活化相结合的方法，研究了洋葱伯克霍尔德菌脂肪酶在大孔树脂NKA上的吸附。酶的比活力为211733.3U/g蛋白，比游离酶粉、非印迹酶和非界面活化酶分别提高了21.7倍、19.4%和47%。该脂肪酶在30 ~ 70 ℃范围内具有良好的热稳定性，对50%浓度的甲醇、乙醇、丙酮等有机溶剂有较强的耐受性。连续使用50批（400 h）后，脂肪酶的活性仍保持在92%以上（甲酯产率从98%降至90%）。圆二色性分析表明，衍生物脂肪酶的活性增强归因于二级结构的变化。本工作中的衍生脂肪酶制剂可能是一个有前途的替代品，以生产令人满意的热稳定性，强溶剂耐受性和高操作重复使用性的生物催化剂。(C)2011 Elsevier B. V.保留所有权利。
The lipase from Burkholderia cepacia adsorbed on macroporous resin NKA was investigated by combined strategies of bioimprinting and interfacial activation to enhance its catalytic performance. The specific activity of the derivative lipase was 211,733.3 U/g-protein, which was 21.7-fold, 19.4% and 47% enhancement over the free lipase powder, non-bioimprinted and non-interfacial activation lipase, respectively. The derivative lipase exhibited a satisfactory thermal stability over a wide range of temperature (from 30 degrees C to 70 degrees C) and a strong tolerance to organic solvents such as methanol, ethanol and acetone with 50% concentration. After being used of 50 successive batches (400h), the derivative lipase still retained over 92% of its original activity (methyl esters yield decreased from 98% to 90%). Circular dichroism analysis indicated that the activity enhancement of the derivative lipase was ascribed to the secondary structure changes. The derivative lipase preparation in this work was probably a promising alternative to produce a biocatalyst of satisfactory thermo-stability, strong solvents tolerance and high operational reusability. (C) 2011 Elsevier B.V. All rights reserved.