Characterization of alpha-galactosidase from Lactobacillus fermentum |
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Authors: | Marisa S Garro Graciela S de Giori Graciela F de Valdez G Oliver |
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Institution: | Centro de Referencia para Lactobacilos (CERELA), Chacabuco 145, Tucumán, Argentina |
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Abstract: | 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 Zn2+ to the reaction buffer exerted a slight negative effect upon the activity, while Hg2+ and p -chloromercuribenzoate produced a strong inhibition. These results would indicate the presence of -SH groups in the catalytic site of the enzyme. |
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