Various dextransucrase molecular mass forms found in enzyme preparations ma
y sometimes be products of proteolytic activity. Extracellular protease in
Leuconostoc mesenteroides strains NRRL B-512F and B-512FMC dextransucrase p
reparations was identified. Protease had a molecular mass of 30 kDa and was
the predominant form derived from a high molecular mass precursor. The pro
duction and activity of protease in culture medium was strongly dependent o
n pH. When L. mesenteroides dextransucrase (173 kDa) was hydrolyzed by prot
ease, at pH 7 and 37 degrees C, various dextransucrase forms with molecular
masses as low as 120 kDa conserving dextransucrase activity were obtained.
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