Immobilization of Pseudomonas cepacia lipase by sol-gel entrapment and its application in the hydrolysis of soybean oil
Immobilization of Pseudomonas cepacia lipase by sol-gel entrapment and its application in the hydrolysis of soybean oil
复制标题
溶胶-凝胶固定化洋葱假单胞菌脂肪酶及其在大豆油水解中的应用
DOI：
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发表时间：
2002
期刊：
影响因子：
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通讯作者：
P. R. Wagner
中科院分区：
文献类型：
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作者：
H. Noureddini;X. Gao;S. Joshi;P. R. Wagner
研究了用化学惰性疏水溶胶载体包埋法固定化洋葱假单胞菌脂肪酶PS的方法。用甲基三甲氧基硅烷（MTMS）、异丁基三甲氧基硅烷（isobtms）和正丁基三甲氧基硅烷水解四甲基氧基硅烷（TMOS）制备凝胶包封脂肪酶。固定化脂肪酶随后用于大豆油的水解，以确定其活性，可回收性和热稳定性。所制备的生物催化剂的水解活性等于或优于游离酶。包埋的脂肪酶的催化活性很大程度上取决于制备过程中所用前体的类型。包埋在TMOS/iso-BTMS内的脂肪酶活性最高。固定化脂肪酶的催化活性在反应的早期阶段更为明显。固定化后脂肪酶的热稳定性显著提高。固定化脂肪酶在70°C时保持稳定，而对于游离酶，在40°C以上观察到中度至严重的活性丧失。固定化脂肪酶始终比游离酶更具有活性和稳定性。固定化的脂肪酶也被证明是非常稳定的，因为在12个1小时的反应后，它保持了95%以上的初始活性。
The immobilization of Lipase PS from Pseudomonas cepacia by entrapment within a chemically inert hydrophobic solgel support was studied. The gel-entrapped lipase was prepared by the hydrolysis of tetramethoxysilane (TMOS) with methyltrimethoxysilane (MTMS), isobutyltrimethoxysilane (iso-BTMS), and n-butyltrimethoxysilane. The immobilized lipase was subsequently used in the hydrolysis of soybean oil to determine its activity, recyclability, and thermostability. The biocatalyst so prepared was equal to or better than the free enzyme in its hydrolytic activity. The catalytic activity of the entrapped lipase strongly depended on the type of precursor that was used in its preparation. The lipase entrapped within TMOS/iso-BTMS showed the highest activity. The catalytic activity of the immobilized lipase was more pronounced during the earlier stages of the reaction. Thermostability of the lipase was significantly improved in the immobilized form. The immobilized lipase was stable up to 70°C, whereas for the free enzyme, moderate to severe loss of activity was observed beyond 40°C. The immobilized lipase was consistently more active and stable than the free enzyme. The immobilized lipase also proved to be very stable, as it retained more than 95% of its initial activity after twelve 1-h reactions.