Frontiers of Chemical Science and Engineering
>> 2016,
Volume 10,
Issue 2
doi:
10.1007/s11705-016-1566-2
RESEARCH ARTICLE
Functional characterization of a thermostable methionine adenosyltransferase from
Beijing Key Laboratory of Bioprocess, Beijing University of Chemical Technology, Beijing 100029, China
Accepted: 2016-04-01
Available online: 2016-05-19
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Abstract
MATTt (a thermostable methionine adenosyltransferase from HB27) was overexpressed in and purified using Ni-NTA affinity column. The enzymatic activity of MATTt was investigated in a temperature range from 30 °C to 90 °C, showing that MATTt exhibited a high enzymatic activity and good thermostability at 80 °C. Circular dichroism spectra reveals that MATTt contains high portion of -sheet structures contributing to the thermostability of MATTt. The kinetic parameter, is 4.19 mmol/L and 1.2 mmol/L for ATP and methionine, respectively. MATTt exhibits the highest enzymatic activity at pH 8. Cobalt (Co ) and zinc ion (Zn ) enhances remarkably the activity of MATTt compared to the magnesium ion (Mg ). All these results indicated that the thermostable MATTt has great potential for industry applications.
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