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. 2015 Nov;50(11):1155-63.
doi: 10.1007/s11745-015-4052-6. Epub 2015 Jul 28.

Purification and Characterization of a Lipase With High Thermostability and Polar Organic Solvent-Tolerance From Aspergillus Niger AN0512

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Purification and Characterization of a Lipase With High Thermostability and Polar Organic Solvent-Tolerance From Aspergillus Niger AN0512

Guang Liu et al. Lipids. .

Abstract

An extracellular lipase (EC 3.1.1.3, AN0512Lip) from Aspergillus niger AN0512 was purified and its characteristics were investigated. After the process of ammonium sulfate precipitation followed by ion-exchange chromatography and gel filtration, the purified lipase was achieved with 203.6-fold purification and 22.1 % recovery. AN0512Lip exhibited the highest activity at 50 °C and pH 5.0. It was thermostable and pH-stable, as indicated by that more than 50 % activity retained at 60 °C for 20 h and more than 90 % activity retained at pH 3.0 for 20 h, respectively. AN0512Lip activity was stimulated by some divalent metal ions (especially Cu(2+), Ca(2+)), while greatly suppressed by EDTA, indicating that AN0512Lip was a metal-activated enzyme. Moreover, AN0512Lip exhibited high tolerance for various polar organic solvents with log P < 0.8, and the highest lipase activity (476 % of its original activity) was achieved after addition of 90 % (V/V) isopropanol to the reaction mixture. AN0512Lip also displayed 3-regiospecificity and great affinity for the long-chain fatty ester. The preliminary test showed that AN0512Lip was a candidate for enriching EPA and DHA in fish oil. All the unique properties, such as thermostability, Cu(2+)-dependent, 3-regiospecificity, and polar organic solvent-tolerance, indicated that AN0512Lip could have potential applications in the food industry, even in organic synthesis and the pharmaceutical industry.

Keywords: Aspergillus niger; Lipase; Polar organic solvent-tolerance; Purification; Thermostable.

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