| Institution: | 1. The State Key Laboratory of Food Science and Technology, School of Food Science and Technology, International Exchange and Cooperation Program, Jiangnan University, Wuxi, Jiangsu 214122, China;2. Robert M. Kerr Food and Agricultural Products Center, Oklahoma State University, Stillwater, OK 74078-6055, USA;3. BaihoBake Biotechnology International, Inc., Nanjing, China;4. Fujian WheatCity Food Development Co., Ltd., Jinjiang, Fujian, China;1. State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, Jiangsu Province, PR China;2. School of Mechanical Engineering, Jiangsu Key Laboratory of Advanced Food Manufacturing Equipment and Technology, Jiangnan University, Wuxi 214122, China;1. Institute of Agrophysics, Polish Academy of Sciences, Do?wiadczalna 4, 20-290 Lublin, Poland;2. Institute of Chemistry, University of Bia?ystok, Cio?kowskiego 1K, 15-245 Bia?ystok, Poland;1. School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China;2. Academy of Contemporary Food Engineering, South China University of Technology, Guangzhou Higher Education Mega Center, Guangzhou 510006, China;3. Engineering and Technological Research Centre of Guangdong Province on Intelligent Sensing and Process Control of Cold Chain Foods, Guangzhou Higher Education Mega Centre, Guangzhou 510006, China;4. Food Refrigeration and Computerized Food Technology, University College Dublin, National University of Ireland, Agriculture and Food Science Centre, Belfield, Dublin 4, Ireland |
| Abstract: | The effects of thermostable ice structuring proteins (TSISPs) extracted from Chinese privet (Ligustrum vulgare) leaves on water molecular state, dehydration of gluten proteins, secondary structure of proteins, glutenin subunit of glutenin macropolymer (GMP) and rheological properties of gluten doughs during frozen storage were investigated by nuclear magnetic resonance (NMR), attenuated total reflectance-Fourier transform infrared reflectance (ATR-FTIR), reversed phase-high performance liquid chromatography (RP-HPLC) and dynamic rheometry. After frozen storage for 5 weeks, the control sample showed dehydration of gluten proteins and mobility of water molecules in gluten dough increased, significantly indicating ice formation and water redistribution. Secondary structure of gluten proteins changed significantly, α-helix decreased and β-sheet increased. Glutenin subunits depolymerized, indicated by the decrease in high molecular weight glutenins/low molecular weight-glutenins (HMW/LMW) ratio. The decrease in elastic moduli (G′) and viscous moduli (G′') showed the deterioration of rheological properties of gluten dough. The addition of TSISPs inhibited the dehydration of gluten proteins, decrease in α-helix, increase in β-sheet and HMW/LMW ratio, resulting in improved rheological properties of gluten dough. |
