Effects of glycation cross-linking reaction on gelling and emulsifying properties of casein
  
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KeyWord:casein  glycation  gelling property  emulsifying property  transglutaminase
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SONG Chunli, CHEN Jiapeng, REN Jian  
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Abstract:
      Transglutaminase was used to catalyze glycation cross-linking reaction of casein and oligochitosan. Three kinds of glycation cross-linked proteins (modified casein) were prepared by controlling reaction time of 1, 2, 4 h. The effects of glycation cross-linking reaction on gelling and emulsifying properties of casein were analyzed. The results showed that the gelation time of the modified casein nearly reduced by 50%. The water holding capacity (centrifugation at 800 r/min for 10 min) of the gel was higher, reaching 99%. The microstructure of the gel changed significantly, and the spatial network structure of the gel was more regular with the reaction time prolonging. The effects of glycation cross-linking reaction on the emulsifying activity and emulsion stability were great.
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