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. 2016 Feb 5;82(4):1004–1014. doi: 10.1128/AEM.02881-15

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FIG 4 — Time course stability of N-deglycosylated and N-glycosylated phytases produced in P. pastoris at pH 2.0 and 37°C over 2 h. (A and B) Residual activities of phytases after acid treatment. For panels A and B, the 100% activity and residual activity were calculated as for Fig. 3; data are represented as means ± SDs. Symbols: □, YrAPPA; ○, YrAPPA-NLT397-399DMK; ■, YkAPPA; ▲, YkAPPA-D397N/K399T; ●, YkAPPA-S200A; , YeAPPA-DMK397-399NLT; △, YeAPPA-A200S; , YeAPPA. (C and D) SDS-PAGE analysis of phytase stability after acid treatment. The phytase band intensity was estimated by using ImageJ software. The untreated phytases were used as the control.

Inline graphic — Time course stability of N-deglycosylated and N-glycosylated phytases produced in P. pastoris at pH 2.0 and 37°C over 2 h. (A and B) Residual activities of phytases after acid treatment. For panels A and B, the 100% activity and residual activity were calculated as for Fig. 3; data are represented as means ± SDs. Symbols: □, YrAPPA; ○, YrAPPA-NLT397-399DMK; ■, YkAPPA; ▲, YkAPPA-D397N/K399T; ●, YkAPPA-S200A; , YeAPPA-DMK397-399NLT; △, YeAPPA-A200S; , YeAPPA. (C and D) SDS-PAGE analysis of phytase stability after acid treatment. The phytase band intensity was estimated by using ImageJ software. The untreated phytases were used as the control.