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Fig. 5 | Biotechnology for Biofuels

Fig. 5

From: Engineering the substrate binding site of the hyperthermostable archaeal endo-β-1,4-galactanase from Ignisphaera aggregans

Fig. 5

IaGal variant overview. In subsite-extended variant 1 and 2 the residues 339–342 were replaced by the sequence ATSYAAEYDPEDAGKWFG with variant 2 having an additional point mutation (R79N). The tryptophan intended as the aromatic platform for binding subsite − 4 is highlighted in bold. Subsite-deleted variant 3 is a point mutation (W388A) while in variant 4 the residue sequence 338–342 has been deleted. The variant nomenclature in the figure is adopted from [32]

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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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