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- Title
Designing of a novel β-galactosidase for production of functional oligosaccharides.
- Authors
Liao, XueYi; Huang, JiaJun; Zhou, QianLing; Guo, LiQiong; Lin, JunFang; You, LinFeng; Liu, Sha; Yang, JingXian
- Abstract
β-galactosidase from L. plantarum FMNP01 was subjected to mutagenesis by domain recombination. A novel β-galactosidase L.pFMNP01Gal-2 was constructed and expressed using the expression vector pET-32a(+) in Escherichia coli BL21 (DE3). The L.pFMNP01Gal-2 was composed of 2406 bp encoding a polypeptide containing 802 amino acids with a predicted molecular mass of 88.22 kDa. When ONPG was used as substrate, the specific activity of L.pFMNP01Gal-2 was 2620 U/g protein, with a K of 2.87 mmol/L and a K of 62.68/s. The optimal temperature and pH for L.pFMNP01Gal-2 were 40 °C and 7.0, respectively. After pre-incubation for 4 h at 40 and 50 °C, respectively, the residual activity of L.pFMNP01Gal-2 retained over 88%. The metal ions Cu and Na had a great inhibitory effect on the activity of L.pFMNP01Gal-2, while other tested metal ions had slight influence. In the presence of lactose and fructose, when L.pFMNP01Gal-2 was used as catalyst, two transfer products were formed during transgalactosylation reaction. It is notable that when L.pFMNP01Gal-2 was used as catalyst with lactose and sucrose as substrates, four transfer products were observed.
- Subjects
GALACTOSIDASES; OLIGOSACCHARIDES; MUTAGENESIS; GENE expression; MOLECULAR weights
- Publication
European Food Research & Technology, 2017, Vol 243, Issue 6, p979
- ISSN
1438-2377
- Publication type
Article
- DOI
10.1007/s00217-016-2813-y