Characterization of a highly stable α-galactosidase from thermophilic Rasamsonia emersonii heterologously expressed in a modified Pichia pastoris expression system

Table 5 Comparison of the effect of metal ions, protein denaturants, and EDTA on the activity of ReGal2 and several thermophilic counterparts

Metal ions and chemicals	Organisms and references
Metal ions and chemicals	Talaromyces emersonii (this study)	Talaromyces leycettanus JCM12802 [12]	Neosartorya fischeri P1 [10]	Penicillium canescens [38]	Agaricus bisporus [39]	Rhizomucor miehei [32]	Thermus thermophiles [31]
Ni²⁺	98.4% (20 mM)	98.5% (5 mM)	98.5% (5 mM)	–	–	90% (2 mM)	–
K⁺	100% (20 mM)	105.9% (5 mM)	77.0% (5 mM)	–	95.3% (10 mM)	102% (2 mM)	–
Mn²⁺	104% (20 mM)	101.2% (5 mM)	103.1% (5 mM)	–	63.9% (10 mM)	95% (2 mM)	20.2% (5 mM)
Cu²⁺	102% (20 mM)	101.1% (5 mM)	93.9% (5 mM)	80% (100 mM)	4.58% (10 mM)	119% (2 mM)	22.2% (5 mM)
Co²⁺	101% (20 mM)	95.6% (5 mM)	95.4% (5 mM)	100% (100 mM)	–	195% (2 mM)	30.1% (5 mM)
Mg²⁺	112% (20 mM)	103.3% (5 mM)	93.6% (5 mM)	–	91.7% (10 mM)	92% (2 mM)	55.6% (5 mM)
Zn²⁺	95% (20 mM)	105.2% (5 mM)	105.0% (5 mM)	100% (100 mM)	95.6% (10 mM)	116% (2 mM)	15.1% (5 mM)
Ca²⁺	106% (20 mM)	98.6% (5 mM)	100.3% (5 mM)	100% (100 mM)	86.9% (10 mM)	129% (2 mM)	27.8% (5 mM)
Ag⁺	0% (5 mM)	0.2% (5 mM)	5.2% (5 mM)	–	0% (10 mM)	4% (2 mM)	–
SDS	104% (200 mM)	0% (5 mM)	19.5% (5 mM)	–	4.53% (50 mM)	5% (2 mM)	1.6% (5 mM)
Urea	109% (200 mM)	–	–	–	–	–	60.0% (5 mM)
GdnHCl	68% (200 mM)	–	–	–	–	–	36.8% (5 mM)
EDTA	100% (200 mM)	103.9% (5 mM)	90.1% (5 mM)	–	106.6% (50 mM)	95% (2 mM)	79.9% (5 mM)
β-Mercaptoethanol	106% (200 mM)	98.6% (5 mM)	77.9% (5 mM)	–	–	–	–

Values represent relative hydrolytic activities of the enzymes in the presence of metal ions or chemicals

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