Domain-swapping of mesophilic xylanase with hyper-thermophilic glucanase

BMC Biotechnology

Table 1 Enzyme property of the chimeras

Enzyme	Xyn Activity			Glu Activity			Physical feature
	t_1/2-50 °C (min)	pH_opt/T_opt(°C)	K_m(mg/ml)/K_cat(s^-1)	t_1/2-95 °C (min)	pH_opt/T_opt(°C)	K_m(mg/ml)/K_cat(s^-1)	MM(kDa) Apparent/Theoretical	Number of residues/pI
Xyn-Glu	47.6	3.8/50	10.2/118.9	> 99.8	3.8/≥ 96	5.9/3.4	53/ 53.2	465/4.5
Glu-Xyn	5.2	3.8/47	44.2/50.2	99.8	5.8/≥ 96	1.88/15.9	53/53.2	467/4.5
Xyn	17.6	3.8/47	12.3/49.2				25/ 21.1	185/4.5
Glu				96.2	3.8/≥ 96	1.87/2.6	29/ 30.9	258/4.78

pH_opt: optimal reaction pH, T_opt: optimal reaction temperature, t_1/2 (min): thermal inactivation half-life, the residual xylanase activity was assayed after incubation at 50 °C at 10-min intervals from 0 – 30 min, and the residual glucanase activity was assayed after incubation at 95 °C at 20-min intervals from 0 – 60 min. K_m and K_cat were determined for birch-wood xylan and carboxymethyl cellulose sodium (CMC).

ISSN: 1472-6750