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  • Title: Purification and some properties of Thermotoga neapolitana thermostable xylanase B expressed in E. coli cells.
    Author: Velikodvorskaya TV, Volkov IYu, Vasilevko VT, Zverlov VV, Piruzian ES.
    Journal: Biochemistry (Mosc); 1997 Jan; 62(1):66-70. PubMed ID: 9113732.
    Abstract:
    A xylanase was purified from the recombinant strain E. coli TG1 carrying the pTT32 vector with a fragment of the Thermotoga neapolitana chromosomal DNA. The enzyme was purified 419-fold with 36% yield after heating at 70 degrees C and pH 4.5 and subsequent ion-exchange chromatography. By polyacrylamide gel electrophoresis in the presence of SDS, the molecular weight of the apparently homogeneous protein is 39 kD. By isoelectric focusing, the protein is of a single form with pI = 5.9. The optimal pH for hydrolysis is 5.5, and the optimal temperature is 90 degrees C. The xylanase is stable to heating at 70 degrees C for 4 h. The enzyme is inactivated by 50% at 80, 90, and 100 degrees C after 227, 162, and 30 min, respectively. Enzyme activity was tested using xylans and glucans as substrates. By thin-layer chromatography of the xylan hydrolysis products, the enzyme was classified as an endoxylanase.
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