Cloning, expression, and purification of a recombinant cold-adapted β-galactosidase from antarctic bacterium Pseudoalteromonas sp. 22b
Protein Expression and Purification, ISSN: 1046-5928, Vol: 39, Issue: 1, Page: 27-34
2005
- 75Citations
- 68Captures
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Metrics Details
- Citations75
- Citation Indexes75
- 75
- CrossRef59
- Captures68
- Readers68
- 68
Article Description
The gram-negative antarctic bacterium Pseudoalteromonas sp. 22b, isolated from the alimentary tract of krill Thyssanoessa macrura, synthesizes an intracellular cold-adapted β-galactosidase. The gene encoding this β-galactosidase has been PCR amplified, cloned, expressed in Escherichia coli, purified, and characterized. The enzyme is active as a homotetrameric protein, and each monomer consists of 1028 amino acid residues. The enzyme was purified to homogeneity (50% recovery of activity) by using the fast, two-step procedure, including affinity chromatography on PABTG–Sepharose. Enzymatic properties of the recombinant protein are identical to those of native Pseudoalteromonas sp. 22b β-galactosidase. The enzyme is cold-adapted and at 10 °C retains 20% of maximum activity. The purified enzyme displayed maximum activity close to 40 °C and at pH of 6.0–8.0. PNPG was its preferred substrate (58% higher activity than against ONPG). The enzyme was particularly thermolabile, losing all activities within 10 min at 50 °C. The hydrolysis of lactose in a milk assay revealed that 90% of milk lactose was hydrolyzed during 6 h at 30 °C and during 28 h at 15 °C. Because of its attributes, the recombinant Pseudoalteromonas sp. 22b β-galactosidase could be applied at refrigeration temperatures for production of lactose-reduced dairy products.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S1046592804003079; http://dx.doi.org/10.1016/j.pep.2004.09.002; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=10644257663&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/15596357; https://linkinghub.elsevier.com/retrieve/pii/S1046592804003079; https://dx.doi.org/10.1016/j.pep.2004.09.002
Elsevier BV
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