Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation
Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation
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DOI：
10.1016/j.fuproc.2012.01.020
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发表时间：
2012-06
影响因子：
7.5
通讯作者：
C. Romero;L. Pera;C. Olivaro;A. Vazquez;M. Baigorí
中科院分区：
文献类型：
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作者：
C. Romero;L. Pera;C. Olivaro;A. Vazquez;M. Baigorí
在燃料工业中使用生物催化剂是一种有趣且更环保的选择。在这一点上，发现黑曲霉MYA 135耐溶剂脂肪酶活性在水解反应和合成反应中的链长选择性取决于酶的制备方法。事实上，在有或没有2%橄榄油的情况下获得的菌丝体结合(Mb)脂肪酶活性，以及在有2%橄榄油的情况下获得的冻干上清液表现出不同的特异性常数(1/α)。因此，在有机介质中，底物专一性最高的是具有组成Mb-脂肪酶的长链脂肪酸(C18；1/α=1.0)。此外，该脂肪酶制剂对酯化反应中棕榈酸甲酯的合成(1/α=1.0 0)和酯交换反应中棕榈酸乙酯的合成(1/α=0.93)具有专一性。有趣的是，诱导的Mb-脂肪酶在酯交换反应(58%的反应发生1/α>；0.5)和酯化反应(88%的反应发生1/α>；0.7)两个反应中都是高活性的生物催化剂。相反，诱导的冻干上清液是在酯化反应中对亚油酸有明显偏好的最特异的酶体系(所有被测试的酰基受体的1/α约为0.77)。
The use of biocatalysts in fuel industry is an interesting and greener alternative. In this connection, it was found that the chain-length selectivity profile of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 determined in both hydrolytic and synthetic reactions depended on the way that the enzyme was prepared. Indeed, a mycelium-bound (Mb) lipase activity obtained either in presence or absence of 2% olive oil as well as a lyophilized supernatant extract obtained in presence of 2% olive oil showed different specificity constants (1/α). Thus, the highest substrate specificity in hydrolysis reaction was observed toward a long-chain fatty acid (C18; 1/α=1.0) with the constitutive Mb-lipase in organic medium. In addition, this lipase preparation was specific toward the synthesis of methyl palmitate during esterification (1/α=1.00) and ethyl palmitate in transesterification (1/α=0.93). Interestingly, the induced Mb-lipase was a highly reactive biocatalyst preparation in both transesterification (58% of the reactions displayed 1/α>0.5) and esterification (88% of the reactions displayed 1/α>0.7) reactions. On the contrary, the induced lyophilized supernatant was the most specific enzymatic system showing a clear preference for linoleic acid in esterification reactions (1/α around of 0.77 for all acyl acceptors tested).