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ARS Home » Research » Publications at this Location » Publication #69030
Title: THE PURIFICATION AND CHARACTERIZATION OF ALTERNANSUCRASE FROM LEUCONOSTOC MESENTEROIDES B-21297

Author
item Ahlgren, Jeffrey
item Cote, Gregory
item Leathers, Timothy

Submitted to: Society of Industrial Microbiology Annual Meeting
Publication Type: Abstract Only
Publication Acceptance Date: 8/4/1996
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Leuconostoc mesenteroides B-21297 is a mutant of L. mesenteroides B-1355 that is essentially free of dextransucrase activity and produces a two-fold increase in the alternansucrase activity. The purification of the extracellular alternansucrase activity from B-21297 incorporated the use of a novel alternanase enzyme to partially degrade endogenous alternan, which significantly enhanced the purification of the alternansucrase by ion exchange chromatography. Electrophoretic analysis of the purified enzyme showed a series of enzymatically active bands that range from 135 to 145 kDa in molecular weight. Preparative electrophoresis was used to prepare individual protein bands for protein microsequencing analysis.