AI Article Synopsis
- - The mature peptide of Aspergillus niger xylanase A was successfully produced in Pichia pastoris, yielding high levels of recombinant AnxA that were secreted into the culture medium.
- - After 96 hours of induction with methanol, the activity of the recombinant enzyme reached 175 U/mg, which is nearly double that of the native enzyme, indicating improved effectiveness.
- - The enzyme displayed optimal performance at 50°C and pH 5.0, showing strong stability across a pH range of 3.0 to 8.0, while primarily producing xylotriose from birchwood xylan during hydrolysis.
Article Abstract
The mature peptide of Aspergillus niger xylanase A (AnxA) was successfully expressed in Pichia pastoris at high levels under the control of AOX1 promoter. The recombinant AnxA (reAnxA) was secreted into culture medium. After 96-h 0.25% methanol induction, the activity of reAnxA in the culture supernatant reached the peak, 175 U/mg, which was 1.9 times as high as that of the native AnxA (92 U/mg). Studies on enzymatic properties showed that the optimum temperature and optimum pH of reAnxA were 50 degrees C and 5.0, respectively. The reAnxA was very stable in a wide pH range of 3.0-8.0. After incubation at the pH 3.0-8.0, 25 degrees C for 1h, all the residual activities of reAnxA were over 80%. The K(m) and k(cat) values for reAnxA were 4.8 mg/ml and 123.2s(-1), respectively. HPLC analysis showed that xylotriose was the main hydrolysis product of birchwood xylan and bran insoluble xylan by reAnxA.
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| http://dx.doi.org/10.1016/j.pep.2006.04.007 | DOI Listing |
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