Proteolytic processing of dextransucrase ofLeuconostoc mesenteroides
1999; Oxford University Press; Volume: 181; Issue: 1 Linguagem: Inglês
10.1111/j.1574-6968.1999.tb08822.x
ISSN1574-6968
AutoresMà nica Sánchez-González, Alejandro Alagà n, Rogelio RodrÃguez-Sotrés, AgustÃn Là pez-MunguÃa,
Tópico(s)Protein Hydrolysis and Bioactive Peptides
ResumoVarious dextransucrase molecular mass forms found in enzyme preparations may sometimes be products of proteolytic activity. Extracellular protease in Leuconostoc mesenteroides strains NRRL B-512F and B-512FMC dextransucrase preparations was identified. Protease had a molecular mass of 30 kDa and was the predominant form derived from a high molecular mass precursor. The production and activity of protease in culture medium was strongly dependent on pH. When L. mesenteroides dextransucrase (173 kDa) was hydrolyzed by protease, 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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