Baking trials were performed with six wheat doughs prepared with xylanase, peroxidase, or glucose oxidase (GOX), and their combinations. Judging dough properties, baking performance, bread volume, and crumb structure, the dough containing xylanase plus peroxidase performed best. Flow relaxation measurements with doughs indicated that peroxidases introduced new transient linkages, whereas glucose oxidase also introduced cross-links permanent on long time scales. Rheological tests and chemical analysis revealed small differences between control and xylanase and/ or peroxidase containing gluten and more pronounced differences for GOX containing gluten. No evidence was found that xylanase specifically removed arabinoxylans from gluten or that peroxidase catalyzed the formation of covalent bonds between arabinoxylans and gluten proteins.
Bread doughs supplemented with xylanase and xylanase plus peroxidase were fractionated into 4 insoluble and 3 soluble fractions. Chemical analysis and high-performance size-exclusion chromatography analysis of apparent molecular weight distribution indicated that xylanase acts on both cold-water-extractable arabinoxylans and on those that can be solubilized from cell wall fragments by hot water extraction. Peroxidase action increased the amount of insoluble small cell wall fragments, notably the amount of protein and arabinoxylan. Arabinoxylans were retained in the small cell wall fragments because cross-linking of arabinoxylans through ferulic acid residues to other arabinoxylans rendered them insoluble. Peroxidase did not affect the composition of gluten, nor was evidence obtained for peroxidase-catalyzed cross-linking of arabinoxylans to protein in the gluten and other fractions.
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