Proteolytic processing of dextransucrase of Leuconostoc mesenteroides.
Various 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.
Sánchez-González
M
M
Instituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo Postal 510-3, Cuernavaca, Morelos, Mexico.
Alagón
A
A
Rodríguez-Sotrés
R
R
López-Munguía
A
A
D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism*; D005964:Glucosyltransferases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007934:Leuconostoc / Q000201:enzymology* / Q000254:growth & development; D011480:Protease Inhibitors / Q000494:pharmacology
D003470:Culture Media; D011480:Protease Inhibitors; D005964:Glucosyltransferases; C020025:dextransucrase; D010450:Endopeptidases