Multifunctional elastin-like polypeptide renders β-glucosidase enzyme phase transition and high stability

Table 1 A comparison of purification efficiency between Ni-NTA resin and ITC

Proteins	Total protein (mg)	Specific activity (unit/mg)	Total activity (unit)	Yield (%)	Purification (fold)
Cell lysate^a (all proteins of E. coli contained EP)	3.25 ± 0.39	0.08 ± 0.004	0.263 ± 0.06
Cell lysate with expression of BglucH^b(all proteins of E. coli contained BglucH)	6.63 ± 0.53	5.75 ± 0.042	37.59 ± 0.89
BglucH^b in cell lysate	6.63 ± 0.53	5.67 ± 0.35*	37.33 ± 0.78	100.0	1.0
BglucLEH^c in cell lysate (all proteins of E. coli contained BglucLEH)	5.23 ± 0.34	6.07 ± 0.46	31.32 ± 0.65
BglucLEH^c in cell lysate	5.23 ± 0.34	5.99 ± 0.54*	31.06 ± 0.63	100.0	1.0
Purified BglucH by Ni-NTA resin	0.41 ± 0.09	68.85 ± 1.19	28.23 ± 0.51	75.62	12.14
Purified BglucLEH by Ni-NTA resin	0.36 ± 0.04	68.22 ± 1.27	24.56 ± 0.59	79.07	11.39
Purified BglucLEH by one round of ITC	0.32 ± 0.05	75.50 ± 1.54	24.16 ± 0.68	77.78	12.60
Purified BglucLEH by two rounds of ITC	0.27 ± 0.03	76.22 ± 1.43	20.58 ± 0.47	66.26	12.72

EP empty plasmid pET-28a(+)
^a,b,c2.5 mL cell extracts was obtained through ultrasonication treatment of E. coli collected from 75 mL LB culture
* Indicates that the specific activity of the empty carrier has been removed

ISSN: 2731-3654