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Fig. 1 | Biotechnology for Biofuels

Fig. 1

From: Discovery, activity and characterisation of an AA10 lytic polysaccharide oxygenase from the shipworm symbiont Teredinibacter turnerae

Fig. 1

Production and stability of TtAA10A. a Architecture of the full-length TtAA10A protein, featuring a signal peptide for secretion (SP), an AA10 LPMO domain, a 70 residue poly-serine linker (predicted to be flexible) and a predicted CBM10. b Architecture of the recombinant TtAA10A core used in this study. c SDS-PAGE of purified TtAA10A (LPMO domain) heterologously produced in E. coli (M molecular weight markers in kDa, P purified protein). d Thermal shift analysis of purified TtAA10A LPMO domain, showing the destabilising effect of copper removal through EDTA treatment, causing a 7.9 °C decrease of the melting temperature

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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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