Cloning and characterization of an exoinulinase from Bacillus polymyxa

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 e...

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Veröffentlicht in:	Biotechnology letters 2003-01, Vol.25 (2), p.155-159
Hauptverfasser:	KWON, Hyun-Ju, JEON, Sung-Jong, YOU, Dong-Ju, KIM, Kwang-Hyeon, JEONG, Yong-Kee, KIM, Young-Hee, KIM, Young-Man, KIM, Byung-Woo
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacillus - classification Bacillus - enzymology Bacillus - genetics Bacillus - isolation & purification beta-Fructofuranosidase Biological and medical sciences Cloning, Molecular Enzyme Activation Escherichia coli - enzymology Escherichia coli - genetics Fructose - biosynthesis Fundamental and applied biological sciences. Psychology Glycoside Hydrolases - biosynthesis Glycoside Hydrolases - chemistry Glycoside Hydrolases - genetics Glycoside Hydrolases - isolation & purification Inulin - metabolism Molecular Sequence Data Molecular Weight Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - genetics Sequence Alignment Soil Microbiology Species Specificity Substrate Specificity
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Zusammenfassung:	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.
ISSN:	0141-5492 1573-6776
DOI:	10.1023/a:1021987923630