Efficient recombinant expression and secretion of a thermostable GH26 mannan endo-1,4-β-mannosidase from Bacillus licheniformis in Escherichia coli

Table 1 Yield of recombinant B. licheniformis mannan endo-1,4-β-mannosidase in different cell compartments of E. coli

Induction	Culture supernatant		Periplasmic Space		Cytoplasm		Total
	4 hr	Ovn	4 hr	Ovn	4 hr	Ovn	4 hr	ovn
*0.1 mM IPTG*
Total Activity (U/L)	8,659	15,076	13,509	9,983	15,189	24,502	37,357	49,561
Total Protein (mg/L)	147	170	44.5	17.8	186	163	378	351
Sp. Activity (U/L)	58.8	89.0	304	560	81.7	150	99.0	141
*0.5 mM IPTG*
Total Activity (U/L)	8,437	14,171	19,649	13,488	10,589	24,480	38,675	52,139
Total Protein (mg/L)	137	156	45.0	20.5	137	199	319	376
Sp. Activity (U/L)	61.7	91.1	437	660	77.3	123	121	139
*1.0 mM IPTG*
Total Activity (U/L)	13,561	14,402	17,647	13,232	24,502	26,632	55,710	54,266
Total Protein (mg/L)	153	175	39.5	20.2	163	168	356	363
Sp. Activity (U/L)	88.9	82.4	447	656	150	159	157	149

The typical yield of the overexpression of recombinant mannan endo-1,4-β-mannosidase from B. licheniformis in E. coli grown in 1-liter shaken flask cultures is reported. Cells were cultivated and enzymes from various compartments were harvested after induction for 4 and 20 h as described in Material and Method.

ISSN: 1475-2859