Cereal Chem 57:111 - 117.  |  VIEW ARTICLE
Defatted and Reconstituted Wheat Flours. VI. Response to Shortening Addition and Lipid Removal in Flours That Vary in Bread-Making Quality.

O. K. Chung, Y. Pomeranz, M. D. Shogren, K. F. Finney, and B. G. Howard. Copyright 1980 by the American Association of Cereal Chemists, Inc. 

Eleven wheat flours that vary in bread-making quality were defatted at 75 C with Skellysolve B or 2- propanol. Skellysolve B extracted 0.93-1.13% unfractionated lipids (0.66-0.79% nonpolar plus 0.24-0.38% polar) and 2-propanol extracted 1.32-1.55% unfractionated lipids (0.68-0.84% nonpolar plus 0.54-0.77% polar). All defatted flours contained only small amounts of residual nonpolar lipids; flours defatted by Skellysolve B contained more residual bound polar lipids than did flours defatted by 2-propanol. Lipid removal increased mixing time; the increase was greater for 2-propanol than for Skellysolve B extraction. Removal of lipids affected mixing time substantially more than did addition of 3% shortening. Small differences in amounts of free polar lipids in flours that vary in bread-making quality accentuated differences in "loaf volume (LV) potential" of flours through the interaction of the free polar lipids and shortening: the better the inherent quality of a flour, the greater the benefits derived from adding shortening. Removal of most of the bound polar lipids may result in improvement of LV in bread baked from propanol- defatted flour without shortening. The amount of improvement was related to the inherent quality of the flours, probably because of differences in their protein quality and protein-protein interactions. We concluded that good LV and crumb grain can be obtained from flours with good protein quality in which adequate protein aggregation is enhanced by free polar lipids that can interact with proteins and shortening. As a mechanism to bring out the maximum LV potential of flours, the multiple interaction of protein-lipid (free polar)-protein in the presence of shortening seems to be superior to the mere formation of protein- protein aggregates.