Interaction of Porcine Myofibrillar Proteins and Various Gelatins: Impacts on Gel Properties

  • Noh, Sin-Woo (Department of Animal Science & Biotechnology, Gyeongnam National University of Science and Technology) ;
  • Song, Dong-Heon (Department of Animal Science & Biotechnology, Gyeongnam National University of Science and Technology) ;
  • Ham, Youn-Kyung (Department of Animal Resources Technology, Gyeongnam National University of Science and Technology) ;
  • Kim, Tae-Kyung (Food Processing Research Center, Korea Food Research Institute) ;
  • Choi, Yun-Sang (Food Processing Research Center, Korea Food Research Institute) ;
  • Kim, Hyun-Wook (Department of Animal Science & Biotechnology, Gyeongnam National University of Science and Technology)
  • Received : 2018.11.28
  • Accepted : 2019.02.25
  • Published : 2019.04.30


The objectives of this study were to determine the interaction between porcine myofibrillar proteins and various gelatins (bovine hide, porcine skin, fish skin, and duck skin gelatins) and their impacts on gel properties of porcine myofibrillar proteins. Porcine myofibrillar protein was isolated from pork loin muscle (M. longissimus dorsi thoracis et lumborum). Control was prepared with only myofibrillar protein (60 mg/mL), and gelatin treatments were formulated with myofibrillar protein and each gelatin (9:1) at the same protein concentration. The myofibrillar protein-gelatin mixtures were heated from $10^{\circ}C$ to $75^{\circ}C$ ($2^{\circ}C/min$). Little to no impacts of gelatin addition on pH value and color characteristics of heat-induced myofibrillar protein gels were observed (p>0.05). The addition of gelatin slightly decreased cooking yield of heat-induced myofibrillar protein gels, but the gels showed lower centrifugal weight loss compared to control (p<0.05). The addition of gelatin significantly decreased hardness, cohesiveness, gumminess, and chewiness of heat-induced myofibrillar gels. Further, sodium dodecyl poly-acrylamide gel electrophoresis (SDS-PAGE) showed no interaction between myofibrillar proteins and gelatin under non-thermal conditions. Only a slight change in the endothermic peak (probably myosin) of myofibrillar protein-gelatin mixtures was found. The results of this study show that the addition of gelatin attenuated the water-holding capacity and textural properties of heat-induced myofibrillar protein gel. Thus, it could be suggested that well-known positive impacts of gelatin on quality characteristics of processed meat products may be largely affected by the functional properties of gelatin per se, rather than its interaction with myofibrillar proteins.


differential scanning calorimetry;duck skin;gelatin;myofibrillar protein gel;porcine


Supported by : Ministry of Agriculture, Food, and Rural Affairs


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