Expression of Endo-1,4-β-mannanase from Penicillium oxalicum in Pichia pastoris

The enzyme Endo-1,4-β-mannanase has a number of applications in different biotechnology industries. Penicillium oxalicum is a powerful hemicellulase-producing fungus, however, few studies have focused on the cloning and expressing endo-1,4-β-mannanase gene from Penicillium oxalicum. The research team of Nanjing Agricultural University's Yangchun Xu cloned the gene from Penicillium oxalicum GZ-2 coding for the enzyme endo-1,4-β-mannanase and expressed it in Pichia pastoris GS115, resulting in the recombinant endo-1,4-β-mannanase (rPoMan5A).

The rPoMan5A is highly thermostable with a half-life of approximately 58 h at 60°C at pH 4.0. The activity of rPoMan5A was not affected by an array of metal ions, but was inhibited by iron and mercury. Analysis of hydrolytic products showed that rPoMan5A could hydrolyze various mannan polymers and release various mannose and manno-oligosaccharides, with the main products being mannobiose, mannotriose, and mannopentaose.

Results demonstrated that expression and secretion of recombinant endo-1, 4-β-mannanase in Pichia pastoris could be suitable for various biotechnology applications.

For more information, read the full article here: http://www.biomedcentral.com/1472-6750/14/90.