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A glucuronoyl esterase from Acremonium alcalophilum cleaves native lignin-carbohydrate ester bonds

Jenny Bååth Arnling (Institutionen för biologi och bioteknik, Industriell bioteknik) ; N. Giummarella ; S. Klaubauf ; M. Lawoko ; Lisbeth Olsson (Institutionen för biologi och bioteknik, Industriell bioteknik)
Febs Letters (0014-5793). Vol. 590 (2016), 16, p. 2611-2618.
[Artikel, refereegranskad vetenskaplig]

The Glucuronoyl esterases (GE) have been proposed to target lignin-carbohydrate (LC) ester bonds between lignin moieties and glucuronic acid side groups of xylan, but to date, no direct observations of enzymatic cleavage on native LC ester bonds have been demonstrated. In the present investigation, LCC fractions from spruce and birch were treated with a recombinantly produced GE originating from Acremonium alcalophilum (AaGE1). A combination of size exclusion chromatography and P-31 NMR analyses of phosphitylated LCC samples, before and after AaGE1 treatment provided the first evidence for cleavage of the LC ester linkages existing in wood.

Nyckelord: P-31 NMR; carbohydrate esterase; lignin-carbohydrate complexes; size exclusion chromatography; spruce and birch



Denna post skapades 2016-11-11.
CPL Pubid: 245060

 

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Institutioner (Chalmers)

Institutionen för biologi och bioteknik, Industriell bioteknik

Ämnesområden

Biokemi och molekylärbiologi
Cellbiologi

Chalmers infrastruktur