alpha-D-galactosidase (EC 3.2.1.22) from Bifidobacterium longum

α‐Galactosidase activity in Bifidobacterium longum was maximal in a range of 40–45°C and at pH of 5.8. At temperatures above 60°C the enzyme was completely inactivated, but it maintained a 100% activity during storage at low temperatures (4, ‐ 30, ‐ 70°C) for 3 months. The addition of Hg2+ to the re...

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Published in:Letters in applied microbiology 1994-07, Vol.19 (1), p.16-19
Main Authors: Garro, M.S, Giori, D.S. de, Valdez, G.F. de, Oliver, G
Format: Article
Language:English
Subjects:
alpha-galactosidase
Bacteriology
Bifidobacterium longum
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
enzyme activity
Fundamental and applied biological sciences. Psychology
Metabolism. Enzymes
Microbiology
Mission oriented research
Physiology and metabolism
purification
starter cultures
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description α‐Galactosidase activity in Bifidobacterium longum was maximal in a range of 40–45°C and at pH of 5.8. At temperatures above 60°C the enzyme was completely inactivated, but it maintained a 100% activity during storage at low temperatures (4, ‐ 30, ‐ 70°C) for 3 months. The addition of Hg2+ to the reaction buffer produced a strong inhibitory effect while Mn2+ exerted a slight positive effect upon activity. The addition of EDTA, inhibitors and other metal ions had no effect on the enzyme α‐galactosidase.
doi_str_mv 10.1111/j.1472-765X.1994.tb00892.x
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source Alma/SFX Local Collection
subjects alpha-galactosidase
Bacteriology
Bifidobacterium longum
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
enzyme activity
Fundamental and applied biological sciences. Psychology
Metabolism. Enzymes
Microbiology
Mission oriented research
Physiology and metabolism
purification
starter cultures
title alpha-D-galactosidase (EC 3.2.1.22) from Bifidobacterium longum
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