Purification, Characterization and N-terminal Protein Sequencing of the Enzyme Dextransucrase Produced by Leuconostoc mesenteroides

 Turki M. Dawoud¹, Fatimah Alshehrei², Khaizran Siddiqui³, Fuad Ameen^1*, Jameela Akhtar³ and Afsheen Arif⁴

¹Department of Botany and  Microbiology, College of Science, King Saud University, Riyadh11451, Saudi Arabia.

²Department of Biology, Jumum college university, Umm Al-Qura University, P.O Box 7388, Makkah 21955, Saudi Arabia.

³Center of Molecular Genetics, University of Karachi, Pakistan.

⁴Karachi Institute of Biotechnology and Genetic Engineering (KIBGE), University of Karachi, Karachi, Pakistan.

Corresponding Author E-mail: fuadameen@ksu.edu.sa

DOI : http://dx.doi.org/10.13005/bbra/2915

ABSTRACT: Background: The wide use of dextran in many different applications, makes its industrial production a challenge and, hence, to obtain a control branched structure of this enzyme research is in progress. Objectives: In the present paper, the enzyme dextransucrase, produced by cultivation of the bacterium Leuconostoc mesenteroides CMG713, was purified and characterized. Methods: The produced dextransucrase was partially purified by PEG400 obtaining a purification factor of 29.4-fold and an overall yield of 18.3% from the initial crude enzymatic extract. Results: The partially purified dextransucrase had a specific activity of 24.0 U/mg and presented a molecular weight of about 200 kDa. In addition, the produced dextransucrase was stable at 30ºC and pH 5.5 for 3 days and led to a highly soluble dextran with wide potential industrial applications.  The current study has successfully partial purification, characterization and conformation of dextransucrase produced by fermentation of the bacterium Leuconostoc mesenteroides CMG713.

KEYWORDS: Dextran; Dextransucrase; Leuconostoc m esenteroides

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