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期刊论文
Aspergillus niger Lipase: Heterologous Expression in Pichia pastoris, MolecularModeling Prediction and the Importance of the Hinge Domains at Both Sidesof the Lid Domain to Interfacial Activation
Biotechnol. Prog., 2009, Vol. 25, No.2,-0001,():
Aspergillus niger lipase (ANL) is an important biocatalyst in the food processing industry.However, there is no report of its detailed three-dimensional structure because of difficultiesin crystallization. In this article, based on experimental data and bioinformational analysisresults, the structural features of ANL were simulated. Firstly, two recombinant ANLsexpressed in Pichia pastoris were purified to homogeneity and their corresponding secondarystructure compositions were determined by circular dichroism spectra. Secondly, the primarystructure, the secondary structure and the three-dimensional structure of ANL weremodeled by comparison with homologous lipases with known three-dimensional structuresusing the BioEdit software, lipase engineering database (http://www.led.uni-stuttgart.de/),PSIPRED server and SwissModel server. The predicted molecular structure of ANL presentedtypical features of the a/b hydrolase fold including positioning of the putative catalytictriad residues and the GXSXG signature motif. Comparison of the predicted threedimensionalstructure of ANL with the X-ray three-dimensional structure of A. niger feruloylesterase showed that the functional difference of interfacial activation between lipase andesterase was concerned with the difference in position of the lid. Our three-dimensionalmodel of ANL helps to modify lipase structure by protein engineering, which will furtherexpand the scope of application of ANL. VVC 2009 American Institute of Chemical EngineersBiotechnol. Prog., 25: 409–416, 2009
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