![]() The characterization of the recombinant TreS of Enterobacter hormaechei suggested its potential application. In this study, several TreS producing strains were screened from a source of soil bacteria. Hg 2+, Zn 2+, Cu 2+and SDS inhibited the enzyme activity at different levels whereas Mn 2+ showed an enhancing effect by 10%. The optimum temperature and pH for the converting reaction were 37☌ and 6, respectively. ![]() ![]() The purified TreS had a molecular mass of 65 kDa and an activity of 18.5 U/mg. The gene was expressed in Escherichia coli, and the recombinant TreS was purified and characterized. The gene contained a 1626 bp open reading frame encoding 541 amino acids. A novel treS gene from Enterobacter hormaechei was amplified using thermal asymmetric interlaced PCR. Six TreS producing strains were isolated from a specimen obtained from soil of the Tibetan Plateau using degenerate PCR. ![]() Therefore, new TreS producing bacteria with suitable enzyme properties are expected to be isolated from extreme environment. This enzymatic process has the advantage of simple reaction and employs an inexpensive substrate. Trehalose synthase (TreS) which converts maltose to trehalose is considered to be a potential biocatalyst for trehalose production. ![]()
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