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Rodriguez, E., Wood, Z.A., Karplus, A. and Lei, X.G. (2000) Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris. Archive for Biochemistry and Biophysics, 382, 105-112. doi:10.1006/abbi.2000.2021.

has been cited by the following article:

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

  AUTHORS: Edward Mullaney, Kandan Sethumadhavan, Stephanie Boone, Xin Gen Lei, Abul H. J. Ullah

  KEYWORDS: Phytase; Disulfide Bridge; Aspergillus niger; Site-Directed Mutagenesis

  JOURNAL NAME: Advances in Biological Chemistry, Vol.2 No.4, November 23, 2012

  ABSTRACT: 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.