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

作者：Peng, Hui^*; Wang, Ying; Zheng, Yunyun; Wang, Min; Xiao, Yazhong; Gao, Yi

来源：Journal of Molecular Catalysis B: Enzymatic , 2013, 98: 114-118.

DOI：10.1016/j.molcatb.2013.10.003

• alpha-Amylase
• Surfactant stable
• Oxidizing agents stable
• Reducing agents stable
• Organic solvent tolerant

The alpha-amylase (AmyP) from a marine metagenomic library shows very low sequence similarity with characterized alpha-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 alpha-amylases capable of resisting toxic compounds, AmyP was the first alpha-amylase with such broad spectrum resistance.

• 出版日期2013-12-30
• 单位安徽大学