, Volume 35, Issue 9, pp 981-990
Date: 24 May 2008

Characterization and large-scale production of recombinant Streptoverticillium platensis transglutaminase

Rent the article at a discount

Rent now

* Final gross prices may vary according to local VAT.

Get Access


Recombinant Streptomyces platensis transglutaminase (MtgA) produced by the Streptomyces lividans transformant 25-2 was purified by ammonium sulfate fractionation, followed by CM-Sepharose CL-6B fast flow, and blue-Sepharose fast flow chromatography. The purification factor was ~33.2-fold, and the yield was 65%. The molecular weight of the purified recombinant MtgA was 40.0 KDa as estimated by SDS-PAGE. The optimal pH and the temperature for the enzyme activity were 6.0 and 55 °C, respectively, and the enzyme was stable at pH 5.0–6.0 and at temperature 45–55 °C. Enzyme activity was not affected by Ca2+, Li+, Mn2+, Na+, Fe3+, K+, Mg2+, Al3+, Ba2+, Co2+, EDTA, or IAA but was inhibited by Fe2+, Pb2+, Zn2+, Cu2+, Hg2+, PCMB, NEM, and PMSF. Optimization of the fermentation medium resulted in a twofold increase of recombinant MtgA activity in both flasks (5.78 U/ml) and 5-l fermenters (5.39 U/ml). Large-scale productions of the recombinant MtgA in a 30-l air-lift fermenter and a 250-l stirred-tank fermenter were fulfilled with maximal activities of 5.36 and 2.54 U/ml, respectively.

Shie-Jea Lin and Yi-Fang Hsieh contributed equally to this work.