title: Use of psychrophilic xylanases provides insight into the xylanase functionality in bread making.
abstract: The bread-improving potential of three psychrophilic xylanases from Pseudoalteromonas haloplanktis TAH3A (XPH), Flavobacterium sp. MSY-2 (rXFH), and unknown bacterial origin (rXyn8) was compared to that of the mesophilic xylanases from Bacillus subtilis (XBS) and Aspergillus aculeatus (XAA). XPH, rXFH, and rXyn8 increased specific bread volumes up to 28%, 18%, and 18%, respectively, while XBS and XAA gave increases of 23% and 12%, respectively. This could be related to their substrate hydrolysis behavior. Xylanases with a high capacity to solubilize water-unextractable arabinoxylan (WU-AX) during mixing, such as XBS and XPH, increased bread volume more than xylanases that mainly solubilized WU-AX during fermentation, such as rXFH, rXyn8, and XAA. Irrespective of their intrinsic bread-improving potential, the dosages needed to increase bread volume to a similar extent were much lower for psychrophilic than for mesophilic xylanases. The xylanase efficiency mainly depended on the enzyme's temperature activity profile and its inhibition sensitivity.
authors.affiliation: Laboratory of Food Chemistry and Biochemistry & Leuven Food Science and Nutrition Research Centre (LFoRCe), Katholieke Universiteit Leuven, Kasteelpark Arenberg 20-bus 2463, B-3001 Leuven, Belgium.
authors.forename: Emmie
authors.initials: E
authors.lastname: Dornez
authors.forename: Priscilla
authors.initials: P
authors.lastname: Verjans
authors.forename: Filip
authors.initials: F
authors.lastname: Arnaut
authors.forename: Jan A
authors.initials: JA
authors.lastname: Delcour
authors.forename: Christophe M
authors.initials: CM
authors.lastname: Courtin
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology*; D001939:Bread; D003296:Cooking / Q000379:methods*; D043364:Endo-1,4-beta Xylanases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D005417:Flavobacterium / Q000201:enzymology*; D005433:Flour; D031161:Pseudoalteromonas / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D043364:Endo-1,4-beta Xylanases