LI-SHENG XU et al: ENZYMATIC SYNTHESIS OF L-2-METHYLTRYPTOPHAN CATALYZED BY ..
نویسندگان
چکیده
L-2-methyltryptophan was prepared from L-serine and 2-methylindole catalyzed by recombinant Escherichia coli with tryptophan synthase activity. In the present research, we used tryptophan synthase (TSase) from recombinant Escherichia coli with pET28a-trpBA plasmid expressing tryptophan synthase from Escherichia coli k-12 MG1655 to produce 2-methyltryptophan, and optimized the conditions for enzymatic synthesis of L-2-methyltryptophan. Under the optimal conditions including 100 mmol/L L-serine, 100 mmol/L 2-methylindole, 1 g tryptophan synthase cells, 0.1mmol/L Ca2+, 50 ml reaction volume, 37 oC, pH = 8.0, the bioconversion rate of L-2-methyltryptophan reached 93% after 6 h.
منابع مشابه
Correction: A new chiral C1-symmetric NHC-catalyzed addition to α-aryl substituted α,β-disubstituted enals: enantioselective synthesis of fully functionalized dihydropyranones.
Chem. Commun., 2015, 51, 8385 | 8385 Cite this:Chem. Commun., 2015, 51, 8385 Correction: A new chiral C1-symmetric NHC-catalyzed addition to a-aryl substituted a,b-disubstituted enals: enantioselective synthesis of fully functionalized dihydropyranones Hong Lu, Jin-Yu Liu, Chen-Guang Li, Jun-Bing Lin, Yong-Min Liang and Peng-Fei Xu* Correction for ‘A new chiral C1-symmetric NHC-catalyzed additi...
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