Literature summary extracted from

Wang, H.; He, W.; Jiang, P.; Yu, Y.; Lin, L.; Sun, X.; Koffas, M.; Zhang, F.; Linhardt, R.J.
Construction and functional characterization of truncated versions of recombinant keratanase II from Bacillus circulans (2017), Glycoconj. J., 34, 643-649 .

Application

EC Number	Application	Comment	Organism
3.2.1.B43	molecular biology	truncated forms of keratanase II exhibit activity and excellent storage and thermal stability making these useful tools for glycobiology research	Niallia circulans

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
3.2.1.B43	synthetic truncated keratanase II gene is subcloned into the NdeI and XhoI sites of pET30a, resulting in the expression construct pKSII, which placed a His6 tag at the extreme C-terminus of the enzyme, expression in Escherichia coli BL21	Niallia circulans

Protein Variants

EC Number	Protein Variants	Comment	Organism
3.2.1.B43	additional information	expression a series of truncation mutants of keratanase II in Escherichia coli BL21 that exhibit activity and excellent storage and thermal stability	Niallia circulans

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.2.1.B43	Niallia circulans	Q7X0Z0	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
3.2.1.B43	6-His tagged keratanase II and its truncated mutants	Niallia circulans

Synonyms

EC Number	Synonyms	Comment	Organism
3.2.1.B43	keratanase II	-	Niallia circulans

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
3.2.1.B43	37	-	assay at	Niallia circulans

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
3.2.1.B43	37	-	2 h, wild-type enzyme shows 66.4% residual activity, truncation mutants show 68.5-100% residual activity	Niallia circulans

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
3.2.1.B43	7	-	assay at	Niallia circulans

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Release 2023.1 (January 2023)