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N -Glycosylation can modulate enzyme structure and function. In this study, we identified two pepsin-resistant histidine acid phosphatase (HAP) phytases fromYersinia kristensenii (YkAPPA) andYersinia rohdei (YrAPPA), each having anN -glycosylation motif, and one pepsin-sensitive HAP phytase fromYersinia enterocolitica (YeAPPA) that lacked anN -glycosylation site. Site-directed mutagenesis was employed to construct mutants by altering theN -glycosylation status of each enzyme, and the mutant and wild-type enzymes were expressed inPichia pastoris for biochemical characterization. Compared with those of theN -glycosylation site deletion mutants andN -deglycosylated enzymes, allN -glycosylated counterparts exhibited enhanced pepsin resistance. Introduction of theN -glycosylation site into YeAPPA as YkAPPA and YrAPPA conferred pepsin resistance, shifted the pH optimum (0.5 and 1.5 pH units downward, respectively) and improved stability at acidic pH (83.2 and 98.8% residual activities at pH 2.0 for 1 h). Replacing the pepsin cleavage sites L197 and L396 in the immediate vicinity of theN -glycosylation motifs of YkAPPA and YrAPPA with V promoted their resistance to pepsin digestion when produced inEscherichia coli but had no effect on the pepsin resistance ofN -glycosylated enzymes produced inP. pastoris . Thus,N -glycosylation may improve pepsin resistance by enhancing the stability at acidic pH and reducing pepsin's accessibility to peptic cleavage sites. This study provides a strategy, namely, the manipulation ofN -glycosylation, for improvement of phytase properties for use in animal feed.

applied and environmental microbiology

<i>N</i> -Glycosylation Improves the Pepsin Resistance of Histidine Acid Phosphatase Phytases by Enhancing Their Stability at Acidic pHs and Reducing Pepsin's Accessibility to Its Cleavage Sites

N -Glycosylation Improves the Pepsin Resistance of Histidine Acid Phosphatase Phytases by Enhancing Their Stability at Acidic pHs and Reducing Pepsin's Accessibility to Its Cleavage Sites