| Institution: | 1. Laboratory of Food Chemistry and Biochemistry and Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 20 Box 2463, B-3001, Heverlee, Belgium;2. Puratos, Industrialaan 25, B-1702, Groot-Bijgaarden, Belgium;3. Nutrex, Achterstenhoek 5, B-2275, Lille, Belgium;1. College of Agronomy, Northwest A & F University, Yangling, Shaanxi 712100, People’s Republic of China;2. School of Veterinary and Life Sciences, Murdoch University, 90, South Street, Murdoch, WA 6150, Australia;3. FBFD PTY LTD, Sydney, Australia;4. Department of Applied Biotechnology and Food Science, BUTE University, Budapest, Hungary;5. Department of Agriculture and Food, Western Australia, 3 Baron-Hay Court, South Perth, WA 6151, Australia |
| Abstract: | Wheat gluten was isolated in a laboratory dough-batter flour separation process in the presence or absence of lipases differing in hydrolysis specificity. The obtained gluten was blended with wheat starch to obtain gluten-starch (GS) blends of which the water and oil binding capacities were investigated. Furthermore, GS blends were mixed into dough and processed into model breads, of which dough extensibility and loaf volume were measured, respectively. In comparison to GS blends prepared with control gluten, oil binding capacity was higher when GS blends contained gluten isolated with Lecitase Ultra (at 5.0 mg enzyme protein/kg flour), a lipase hydrolyzing both non-polar and polar lipids. Additionally, dough extensibility and total work needed for fracture were lower for dough prepared from GS blends containing gluten isolated with Lipolase (at 5.0 mg enzyme protein/kg flour), a lipase selectively degrading non-polar lipids. In GS blend bread making, this resulted in inferior loaf volumes. Comparable GS blend properties were measured when using control gluten and gluten isolated with YieldMAX, a lipase mainly degrading N-acyl phosphatidylethanolamine. In conclusion, properties of GS blend model systems are altered when gluten prepared in the presence of lipases is used to a degree which depends on lipase specificity and concentration. |
