Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation

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• 作者：Cintia M. Romero^a ; Licia M. Pera^a ; Cristina Olivaro^b ; ¹ ; Alvaro Vazquez^b ; ¹ ; Mario D. Baigori^a ; ^{lymb32@gmail.com.ar}
• 关键词：Substrate specificity ; Lipase ; Biodiesel component ; Aspergillus niger ; Whole-cell
• 刊名：Fuel Processing Technology
• 出版年：2012
• 期刊代码：36_03783820
• 类别：ce
• 出版时间：June, 2012
• 卷：98
• 期：Complete
• 页码：23-29
• 文件大小：312 K

摘要

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/伪). Thus, the highest substrate specificity in hydrolysis reaction was observed toward a long-chain fatty acid (C18; 1/伪 = 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/伪 = 1.00) and ethyl palmitate in transesterification (1/伪 = 0.93). Interestingly, the induced Mb-lipase was a highly reactive biocatalyst preparation in both transesterification (58%of the reactions displayed 1/伪 > 0.5) and esterification (88%of the reactions displayed 1/伪 > 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/伪 around of 0.77 for all acyl acceptors tested).