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Chinese Journal of Biotechnology ; (12): 860-867, 2011.
Article in Chinese | WPRIM | ID: wpr-324493

ABSTRACT

Based on previous bioinformational analysis results, two Aspergillus niger lipase (ANL) mutants, ANL-Ser84Gly and ANL-Asp99Pro were constructed to screen ANL mutants with oil-water interface independence. ANL-Ser84Gly still displayed a pronounced interfacial activation, while ANL-Asp99Pro displayed no interfacial activation. The specific activity of ANL-Ser84Gly towards p-nitrophenyl palmitate (-myristate, -laurate and -decanoate) decreased by 29.8% (53.1, 60.1 and 77.1, respectively) than that of ANL, while the specific activity of ANL-Asp99Pro towards p-nitrophenyl palmitate increased by 2.2-fold. The mutation in the hinge region at both sides of the lid domain also destabilized various secondary structure factors of ANL-S84G and ANL-D99P, which resulted in a substantial decrease in thermostability. The achievement to construct oil-water interface-independent ANL mutants would help to further understand lipase interfacial activation mechanism.


Subject(s)
Aspergillus niger , Genetics , Base Sequence , Enzyme Stability , Fungal Proteins , Genetics , Metabolism , Lipase , Genetics , Metabolism , Molecular Sequence Data , Mutant Proteins , Genetics , Oils , Substrate Specificity , Water
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