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Characterization of alpha‐galactosidase from Lactobacillus fermentum
Author(s) -
Garro Marisa S.,
Giori Graciela S.,
Valdez Graciela F.,
Oliver G.
Publication year - 1993
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1993.tb02805.x
Subject(s) - lactobacillus fermentum , enzyme , strain (injury) , chemistry , enzyme assay , alpha galactosidase , lactobacillaceae , catalysis , lactobacillus , nuclear chemistry , biochemistry , food science , lactic acid , bacteria , biology , fermentation , medicine , genetics , anatomy , lactobacillus plantarum , fabry disease , disease
α‐Galactosidase activity was studied in Lactobacillus fermentum strains. The optimum temperature was found to be 45°C. The enzyme was inactivated at temperatures higher than 55°C, but remained active during storage at low temperatures (0, ‐30 and ‐70°C) for 5 months. Enzyme activity was observed within a 5.0–6.5 pH range, while optimum pH was dependent on the particular strain assayed. The addition of Zn 2+ to the reaction buffer exerted a slight negative effect upon the activity, while Hg 2+ and p ‐chloromercuribenzoate produced a strong inhibition. These results would indicate the presence of ‐SH groups in the catalytic site of the enzyme.