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Title: Cloning and characterization of an exoinulinase from Bacillus polymyxa. Author: Kwon HJ, Jeon SJ, You DJ, Kim KH, Jeong YK, Kim YH, Kim YM, Kim BW. Journal: Biotechnol Lett; 2003 Jan; 25(2):155-9. PubMed ID: 12882292. Abstract: A gene encoding an exoinulinase (inu) from Bacillus polymyxa MGL21 was cloned and sequenced. It is composed of 1455 nucleotides, encoding a protein (485 amino acids) with a molecular mass of 55,522 Da. Inu was expressed in Escherichia coli and the His-tagged exoinulinase was purified. The purified enzyme hydrolyzed sucrose, levan and raffinose, in addition to inulin, with a sucrose/inulin ratio of 2. Inulinase activity was optimal at 35 degrees C and pH 7, was completely inactivated by 1 mM Ag+ or Hg2+. The Km and Vmax values for inulin hydrolysis were 0.7 mM and 2500 microM min(-1) mg(-1) protein. The enzyme acted on inulin via an exo-attack to produce fructose mainly.[Abstract] [Full Text] [Related] [New Search]