| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1955396 | Biophysical Journal | 2009 | 12 Pages |
Abstract
The Thermomyces lanuginosa lipase has been extensively studied in industrial and biotechnological research because of its potential for triacylglycerol transformation. This protein is known to catalyze both hydrolysis at high water contents and transesterification in quasi-anhydrous conditions. Here, we investigated the Thermomyces lanuginosa lipase structure in solution in the presence of a tributyrin aggregate using 30 ns molecular-dynami
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
S. Santini, J.M. Crowet, A. Thomas, M. Paquot, M. Vandenbol, P. Thonart, J.P. Wathelet, C. Blecker, G. Lognay, R. Brasseur, L. Lins, B. Charloteaux,