Covalent immobilization of Candida rugosa lipase on aldehyde functionalized hydrophobic support and the application for synthesis of oleic acid ester
Covalent immobilization of Candida rugosa lipase on aldehyde functionalized hydrophobic support and the application for synthesis of oleic acid ester
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DOI：
10.1080/09205063.2013.786970
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发表时间：
2013-08
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影响因子：
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通讯作者：
Zülfikar Temoçin
中科院分区：
文献类型：
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作者：
Zülfikar Temoçin
研究了聚对苯二甲酸乙二酯接枝甲基丙烯酸缩水甘油酯（PET-g-GMA）纤维共价固定化皱褶假丝酵母脂肪酶（CRL）。固定化产生2.38mg g-1的PET-g-GMA纤维的蛋白质负载。以橄榄油的水解和油酸的酯化反应为例，对固定化和游离CRL的性能进行了评价。通过固定化将CRL的最佳活性pH改变至中性范围。游离和固定化CRL的最大活性分别出现在40和45 °C。固定化脂肪酶在50 °C下反应2 h，酶活力保持65%。结果发现，储存在4 °C下的固定化脂肪酶在35天后保留了其原始活性的90%，而储存在4 °C下的游离脂肪酶在同一时期后保留了其原始活性的69%。在酯化实验中，固定化CRL在含水量为1.5 ~ 6%（v/v）时仍能保持较高的活性，而游离CRL的活性则表现出明显的含水量依赖性，当含水量超过3%（v/v）时活性迅速下降。此外，在5次重复使用后，固定化CRL的酯化率从29%略微下降到27%。
This study focuses on Candida rugosa lipase (CRL) immobilization by covalent attachment on poly(ethylene terephthalate)-grafted glycidyl methacrylate (PET-g-GMA) fiber. The immobilization yielded a protein loading of 2.38 mg g-1 of PET-g-GMA fiber. The performances of the immobilized and free CRLs were evaluated with regard to hydrolysis of olive oil and esterification of oleic acid. The optimum activity pH of the CRL was changed by immobilization to neutral range. The maximum activity of the free and immobilized CRLs occurred at 40 and 45 °C respectively. The immobilized lipase retained 65% of its original activity at 50 °C for 2 h. It was found that the immobilized lipase stored at 4 °C retained 90% of its original activity after 35 days, whereas the free lipase stored at 4 °C retained 69% of its original activity after the same period. In the esterification experiments, the immobilized CRL could maintain a high activity at a water content range from 1.5 to 6% (v/v), while the activity of free CRL showed a clear dependence on water content and decreased rapidly at above 3% (v/v) water content. In addition, after five reuses, the esterification percent yield of the immobilized CRL slightly decreased from 29 to 27%.