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Effects of Commercial Hydrolytic Enzyme Additives on Japanese-Style Sponge and Dough Bread Properties and Processing Characteristics

May 2005 Volume 82 Number 3
Pages 314 — 320
O. Harada , 1 E. D. Lysenko , 2 N. M. Edwards , 2 , 3 and K. R. Preston 2

Yamazaki Baking Co., Research and Development Division, 3-15-6 Chitose, Sumida-Ku, Tokyo 130-0025, Japan. Canadian Grain Commission, Grain Research Laboratory, 1404-303 Main Street, Winnipeg, MB, Canada R3C 3G8. Contribution No. 878. Corresponding author. E-mail: nedwards@grainscanada.gc.ca


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Accepted January 13, 2005.
ABSTRACT

The effects of increasing levels of eight commercial fungal enzymes enriched in four types of activity (α-amylase, protease, xylanase, or cellulase) on Japanese-style sponge and dough bread quality and processing characteristics have been studied using a Canadian red spring wheat straight-grade flour. At optimum levels, the enriched α-amylases, xylanases, and cellulases increased loaf volume and bread score and reduced crumb firmness, while the proteases only reduced crumb firmness. For α-amylases, xylanases, and cellulases, optimum levels for crumb firmness were obtained at higher levels of addition than for loaf volume and bread score. At high levels of addition, all four enriched enzyme types reduced loaf volume and bread score and increased crumb firmness relative to optimum levels, with the proteases showing the most dramatic effects. α-Amylases and cellulases had little impact on dough mixing requirements, while xylanases increased and proteases greatly reduced mixing requirements. All enzymes at optimum levels reduced sheeting work requirements, resulting in softer more pliable dough. Optimum bread properties for α-amylases, xylanases, and cellulases were attained within a relatively narrow range of dough sheeting work values. This similarity in response suggests a dominant common nonspecific mechanism for their improver action, which is most likely related to water release and the resulting impact on physical dough properties.



This article is in the public domain and not copyrightable. It may be freely reprinted with customary crediting of the source. AACC International, Inc., 2005.