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In this study, the optimum temperature was lowered while the residual phytase activity after heating to 70℃ was raised in a widely utilized phytase, <i>Aspergillus niger</i> 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

advances in biological chemistry

Elimination of a disulfide bridge in &amp;lt;i&amp;gt;Aspergillus niger&amp;lt;/i&amp;gt; NRRL 3135 Phytase (PhyA) enhances heat tolerance and optimizes its temperature versus activity profile