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Effect of transglutaminase on rheological properties and microstructure of chemically acidified sodium caseinate gels
Affiliation:1. Department of Food Science and Technology and KLGPNPS, South China University of Technology, Guangzhou 510640, People''s Republic of China;2. State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou 510640, People''s Republic of China;1. Young Researchers and Elites Club, Lahijan Branch, Islamic Azad University, Lahijan, Iran;2. Nano-Bio Science Research Group, DTU-Food, Technical University of Denmark, Kemitorvet B 202, 2800 Kgs. Lyngby, Denmark;1. Institute of Molecular, Cell and Systems Biology, University of Glasgow, Glasgow, G12 8QQ, UK;2. Research School of Chemistry, The Australian National University, Acton, ACT 2601, Australia;1. Teagasc Food Research Centre, Moorepark, Fermoy, Co. Cork, Ireland;2. School of Food and Nutritional Sciences, University College Cork, Cork, Ireland
Abstract:The mechanical properties and microstructure of 2.7% and 4.5% sodium caseinate gels chemically acidified by glucono-δ-lactone (GDL) and cross-linked by microbial transglutaminase (TG) were studied. The acidification was performed at different temperatures. According to SDS–PAGE TG clearly caused polymerisation of caseinate irrespective of the treatment temperature (4–50 °C), The cross-linking of the proteins was more extensive at temperatures 22–50 °C. Low amplitude viscoelastic measurements showed that 4.5% caseinate gels acidified at 50 °C were formed much faster than gels acidified at 22 °C. TG only slightly increased the time of gelling. Control gels prepared without TG at temperatures of 4, 22, 37 and 50 °C were mechanically weak. Examination of the control gels with a confocal laser scanning microscope showed that gels formed at 37 and 50 °C were coarse and porous with large cavities between particle aggregates, whereas those formed at 22 °C were much more homogeneous. The TG-treated and acidified sodium caseinate dispersions formed firm gels, indicating cross-linking of casein proteins. Interestingly, the strongest gels were formed at 22 and 37 °C. TG treatment improved the homogeneity of the gel structure at temperatures of 37 and 50 °C. The hardness of TG-treated gels acidified at 4 °C increased during 1 week of storage.
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