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Solubilization of Arabinoxylans from Isolated Water‐Unextractable Pentosans and Wheat Flour Doughs by Cell‐Wall‐Degrading Enzymes
Author(s) -
PetitBenvegnen M.D.,
Saulnier L.,
Rouau X.
Publication year - 1998
Publication title -
cereal chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.558
H-Index - 100
eISSN - 1943-3638
pISSN - 0009-0352
DOI - 10.1094/cchem.1998.75.4.551
Subject(s) - arabinoxylan , chemistry , cellulase , food science , enzyme , trichoderma reesei , esterase , aspergillus niger , biochemistry , glycoside hydrolase , polysaccharide
Water‐unextractable pentosans (WUP) isolated from the flours of three wheat cultivars (Apollo, Soissons, Thésée) were treated with enzymes to solubilize the arabinoxylans. The water‐unextractable arabinoxylans from the three cultivars had similar susceptibility to solubilization by enzymes: Grindamyl S 100 (GS100), a commercial preparation for baking, rich in pentosanase activities that originated from an Aspergillus niger culture; and three endoxylanases (E1, E2, E3), an arabinofuranosidase (Af), a β‐ glucanase (βG), and a ferulate esterase (FAE) purified from GS100. A cellulase (C) and a pure endoglucanase (eG) from Trichoderma reesei were also used. GS100 was able to solubilize high molecular weight arabinoxylans (HMWAX) from WUP that markedly enhance the viscosity of the reaction mixture supernatants. The endoxylanase E1 was responsible for this solubilizing activity of GS100, whereas E2 and E3 made only a very low contribution. Combining E1 with FAE led to a limited increase in the arabinoxylan‐solubilizing effect. Also, enzymes hydrolyzing cellulose and β‐glucans slightly improved the arabinoxylan solubilization from WUP when combined with GS100 or E1, but produced arabinoxylans of lower intrinsic viscosity. Similar effects of the enzymes were observed on arabinoxylan solubilization when applied to dough instead of isolated WUP.