α-Amylase (AmyP) of glycoside hydrolase subfamily GH13_37 is resistant to various toxic compounds

•The amylase AmyP was very stable toward surfactants, oxidants, reducers and organic solvents.•The activity of AmyP was strongly stimulated by Cu2+.•The activity of AmyP was enhanced by 25% of n-octanol.

The α-amylase (AmyP) from a marine metagenomic library shows very low sequence similarity with characterized α-amylases and belongs to a new glycoside hydrolase subfamily GH13_37. This amylase retained above 87% residual activity in the presence of metal ions (concentrations <10 mM) tested except Hg2+ and was strongly stimulated by 5 mM Cu2+. AmyP was active over a wide range of salt concentration (0–3 M) with the optimal concentration at 1 M. The enzyme exhibited 119, 106, 108, 42 and 31% of its activity the presence of 2% Tween 20, Tween 40, Triton X-100, SDS and CTAB, respectively, showing excellent resistance. Oxidizing agents (H2O2 and NaClO3) not strongly inactivated the enzyme. DTT was found to greatly enhance the activity (to 198% of original activity), while 2-mercaptoethanol had no significant effect on the enzyme. Moreover, AmyP retained considerable activity in both hydrophobic solvents and hydrophilic solvents, and n-octanol even increased the amylase activity to 113%. Compared to other α-amylases capable of resisting toxic compounds, AmyP was the first α-amylase with such broad spectrum resistance.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slide