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Elimination of a disulfide bridge in Aspergillus niger NRRL 3135 Phytase (PhyA) enhances heat tolerance and optimizes its temperature versus activity profile

Author(s): Edward Mullaney | Kandan Sethumadhavan | Stephanie Boone | Xin Gen Lei | Abul H. J. Ullah

Journal: Advances in Biological Chemistry
ISSN 2162-2183

Volume: 02;
Issue: 04;
Start page: 372;
Date: 2012;
Original page

Keywords: Phytase | Disulfide Bridge | Aspergillus niger | Site-Directed Mutagenesis

In this study, the optimum temperature was lowered while the residual phytase activity after heating to 70℃ was raised in a widely utilized phytase, Aspergillus niger NRRL 3135 PhyA. This was accomplished by site-directed mutagenesis of the cysteines that are involved in the formation of a single disulfide bridge (DB). When compared to wild type (WT), three of the four mutant phytases displayed a lower optimum temperature, 42℃, and up to a four-fold increase in activity after heating. These findings have a potentially broad application to be incorporated along with other desirable features to engineer a phytase with superior physical and chem-ical attributes for animal feed applications.
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