Heterologous expression, purification and characterization of nitrilase from Aspergillus niger K10
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چکیده
منابع مشابه
Retraction: Heterologous expression, purification and characterization of nitrilase from Aspergillus niger K10
Retraction The authors have retracted this article [1] due to the ethical misconduct of Karel Bezouska and misappropriation of data which fundamentally changes the main findings of the article. Specifically, the upper amino acid sequence in Figure 1 (by KB) in BMC Biotechnol 11:2 was incorrect, therefore Nit-ANigWT and Nit-ANigRec (nitrilase expressed in E. coli harbouring a nit gene from A. ni...
متن کاملHeterologous expression, purification and characterization of nitrilase from Aspergillus niger K10
BACKGROUND Nitrilases attract increasing attention due to their utility in the mild hydrolysis of nitriles. According to activity and gene screening, filamentous fungi are a rich source of nitrilases distinct in evolution from their widely examined bacterial counterparts. However, fungal nitrilases have been less explored than the bacterial ones. Nitrilases are typically heterogeneous in their ...
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The enzyme pgalactosidase from a mutant strain of A. niger UV-5 was partially purified using ammonium sulfate and acetone. The saturation range of 60-80% ammonium sulfate was found to yield 60.5% enzyme recovery with 2.4 fold purification. Acetone precipitation at enzyme: acetone ratio of 1 : 1.5 brought about a higher yield i.e. 68% and three-fold purification. The combined procedures of ...
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In this study, Aspergillus niger lipase after extraction of medium culture was precipitated with different percentages of acetone and purified by ion exchange chromatography using SP-sepharose HP and Q-sepharose HP. The process of purification of the anzyme was studied by electrophoresis and the molecular weight was detected and determined by Zymography using overlying containing phenol red and...
متن کاملPurification, characterization, and heterologous expression in Fusarium venenatum of a novel serine carboxypeptidase from Aspergillus oryzae.
A novel serine carboxypeptidase (EC 3.4.16.1) was found in an Aspergillus oryzae fermentation broth and was purified to homogeneity. This enzyme has a molecular weight of ca. 67,000, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its specific activity is 21 U/mg for carbobenzoxy (Z)-Ala-Glu at pH 4.5 and 25 degrees C. It has a ratio of bimolecular constants for ...
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ژورنال
عنوان ژورنال: BMC Biotechnology
سال: 2011
ISSN: 1472-6750
DOI: 10.1186/1472-6750-11-2