Effects of konjac glucomannan on heat-induced changes of physicochemical and structural properties of surimi gels |
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| Affiliation: | 1. Department of Seafood Processing, Faculty of Marine Sciences, Tarbiat Modares University, Noor, Iran;2. Department of Fisheries, University of Agricultural Sciences and Natural Resources, Gorgan, Iran;1. Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Key Laboratory of Functional Food from Plant Resources, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, PR China;2. School of Food and Chemical Engineering, Beijing Technology and Business University, No. 33, Fucheng Road, Beijing 100048, PR China;3. Japan International Research Center for Agricultural Sciences, Tsukuba 305-8686, Japan;1. State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 214122, China;2. Fujian Anjoyfood Share Co. Ltd., Xiamen, 361022, China;3. National Engineering Research Center for Functional Food, Jiangnan University, Wuxi, 214122, China;4. School of Food Science and Technology, Jiangnan University, Wuxi, 214122, China;5. Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Wuxi, 214122, China |
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| Abstract: | This work demonstrated the protective effects of konjac glucomannan (KGM) on the physicochemical and structural properties of surimi gels subjected to 120 °C. The T2 relaxation of LF-NMR which was used to detect water mobility, changed more obviously with the addition of deacetylated KGM than with the native, which indirectly implied that deacetylated KGM more pronouncedly influenced the protein structure. Hydrophobic interaction, ionic, hydrogen, and disulfide bonds, were sheltered by deacetylated KGM to greater extent than by native KGM. Raman spectra showed that the reduction of the main random-coil secondary protein structure at 120 °C was more significantly mitigated by deacetylated KGM. The interactions between protein and native or deacetylated KGM were investigated by X-ray diffraction, finding that protein and polysaccharide complexes might be formed. The microstructure of the mixed gels, determined by confocal laser scanning microscopy, demonstrated native and deacetylated KGM helped protein aggregation recover to uniform distribution. |
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