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Enzyme Microb Technol. 2017 Oct;105:30-37. doi: 10.1016/j.enzmictec.2017.06.007. Epub 2017 Jun 12.

Hydration-aggregation pretreatment for drastically improving esterification activity of commercial lipases in non-aqueous media.

Author information

1
Faculty of Engineering, Tokyo City University, 1-28-1 Tamazutsumi, Setagaya-ku, Tokyo, 158-8557, Japan.
2
Faculty of Engineering, Tokyo City University, 1-28-1 Tamazutsumi, Setagaya-ku, Tokyo, 158-8557, Japan. Electronic address: tkuroiwa@tcu.ac.jp.
3
School of Bioscience and Biotechnology, Tokyo University of Technology, 1404-1 Katakura-cho, Hachioji, Tokyo, 192-0982, Japan.

Abstract

We investigated a novel, simple method for activating lipases in non-aqueous reaction media. Lipase powders were suspended in n-fatty alcohols and were then hydrated by adding a small amount of water. A paste-like aggregate was recovered from the mixture followed by lyophilization for obtaining activated lipases as dry powders. Lipase activity was evaluated for esterification between myristic acid and methanol in n-hexane. The activated lipases exhibited high esterification activity depending on the experiment conditions during hydration-aggregation pretreatment such as the amount of added water, the temperature, the pH of added buffer solutions, and the carbon chain length of the n-fatty alcohols used as pretreatment solvents. Various commercial lipases from different origins could be activated by this method. Changes in lipase conformation induced by the hydration-aggregation pretreatment were studied based on fluorescence and Fourier-transform infrared spectroscopy.

KEYWORDS:

Interfacial activation; Lipase-catalyzed esterification; Lyophilization; Non-aqueous enzymology; Organic solvent

PMID:
28756858
DOI:
10.1016/j.enzmictec.2017.06.007
[Indexed for MEDLINE]

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