Purification and characterization of hydrolytic and transgalactosyl α-galactosidase from Lactobacillus helveticus ATCC 10797

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  1. Get@NRC: Purification and characterization of hydrolytic and transgalactosyl α-galactosidase from Lactobacillus helveticus ATCC 10797 (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1007/s00217-014-2284-y
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TypeArticle
Journal titleEuropean Food Research and Technology
ISSN1438-2377
Abstractα-Galactosidase purified from Lactobacillus helveticus ATCC 10797 by fast performance liquid chromatography system using ion exchange and gel-filtration columns showed the Km of 3.83 mM and Vmax of 416.44 μmol/min/mg protein calculated from the substrate p-nitrophenyl-α-d-galactopyranoside. The molecular mass was 188 kDa by gel-filtration, but 90 kDa by SDS-PAGE, indicating a homodimer. The optimum temperature was 37 °C, and the optimum pH was at 6 with an acceptable stability between pH 4 and 8. This enzyme was activated by 10 mM monovalent ions such as K+, NH4 +, Li+, and CS+, while the activity was inhibited by divalent ions such as Cu2+, Zn2+, and Fe2+. Melibiose was hydrolyzed to glucose and galactose, raffinose to galactose and sucrose, while stachyose to galactose and sucrose. A novel source of α-galactosidase from L. helveticus possessing both hydrolytic activity to eliminate flatulence sugars and transgalactosylation activities to synthesize galacto-oligosaccharides is identified and characterized. © 2014 Springer-Verlag Berlin Heidelberg.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); Human Health Therapeutics (HHT-TSH)
Peer reviewedYes
NPARC number21272262
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Record identifierdeb0cba9-3b39-4814-8729-fb47ebb63a13
Record created2014-07-23
Record modified2016-05-09
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