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- Publisher
- Springer Journals
- Copyright
- Copyright © 2008 by Springer-Verlag
- Subject
- Chemistry; Microbial Genetics and Genomics; Microbiology ; Biotechnology
- ISSN
- 0175-7598
- eISSN
- 1432-0614
- DOI
- 10.1007/s00253-008-1750-5
- pmid
- 19005653
- Publisher site
- See Article on Publisher Site
Abstract
A genomic library of Bifidobacterium bifidum (NCIMB 41171) DNA was constructed in Escherichia coli RA11r (melA−B+) and one α-galactosidase encoding gene was isolated. Conceptual translation combined with insertional mutagenesis analysis indicated an open reading frame (ORF) of 759 amino acid (aa) residues encoding an α-galactosidase (named as MelA) of 82.8 kDa. Partial purification and characterisation showed that the enzyme had an apparent native molecular mass of ≈243 kDa and a subunit size of ≈85 kDa. The enzyme belongs to glycosyl hydrolases 36 family with high aa sequence similarities (≈73%) to other known α-galactosidases of bifidobacterial origin. Under optimum pH conditions for activity (pH 6.0) and high melibiose concentration (40% w/v), the enzyme was able to form oligosaccharides with degree of polymerisation (DP) ≥3 at higher concentration than DP = 2, with a total yield of 20.5% (w/w).
Journal
Applied Microbiology and Biotechnology – Springer Journals
Published: Nov 13, 2008