Article ID Journal Published Year Pages File Type
17157 Enzyme and Microbial Technology 2013 8 Pages PDF
Abstract

Myriococcum thermophilum cellobiose dehydrogenase (MtCDH) was expressed in Pichia pastoris using the pPICZαA expression vector under the control of methanol inducible AOX promoter. The purified recombinant MtCDH with a specific activity of 3.1 U mg−1 was characterized to obtain kinetic constants for various carbohydrate substrates. Additionally, the C1 oxidation of the reducing ends of cellobiose, cellotetraose and maltotriose by MtCDH was verified by HPLC-MS. MtCDH was employed to oxidize several different cellulose-based materials by production of hydrogen peroxide. Based on the obtained results a one-pot enzymatic scouring/bleaching process for cotton fabrics was developed using pectinases as scouring agent and MtCDH to produce H2O2 for bleaching. An average increase in whiteness (Berger) ΔE of 26 and an average 95% increase in wettability were observed in all MtCDH treated fabrics. In addition, MtCDH oxidized typical colored cotton flavonoids (morin, rutin, isoquercitrin).

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► We investigate the possibility of using cellobiose dehydrogenase for bleaching cotton. ► Investigate over expression of recombinant Myriococcum thermophilum cellobiose dehydrogenase in Pichia pastoris. ► Cellobiose dehydrogenase oxidized a variety of oligosaccharides present in desizing liquors. ► Simultaneous production of H2O2 and bleaching was more effective.

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Physical Sciences and Engineering Chemical Engineering Bioengineering
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