Mung Bean Trypsin Inhibitor Is Effective in Suppressing the Degradation of Myofibrillar Proteins in the Skeletal Muscle of Blue Scad (Decapterus maruadsi)
2010
Sun, Le-Chang | Yoshida, Asami | Cai, Qui-Feng | Liu, Guang-Ming | Weng, Ling | Tachibana, Katsuyasu | Su, Wen-Jin | Cao, Min-Jie
Mung bean trypsin inhibitor (MBTI) of the Bowman−Birk family was purified to homogeneity with a molecular mass of approximately 9 kDa on tricine−sodium dodecyl sulfate−polyacrylamide gel electrophoresis (SDS−PAGE) and 8887.25 Da as determined by matrix-assisted laser desorption/ionization−quadrupole ion trap−time-of-flight mass spectrometry (MALDI−QIT−TOF MS). Using blue scad myofibrillar proteins as targets, it was found that, in the absence of MBTI, proteolysis of myofibrillar proteins, especially myosin heavy chain (MHC), could be identified after incubation at 55 °C for 2 h, while in the presence of MBTI, with a final concentration of 25 ng/mL, proteolysis of these proteins was greatly suppressed even after incubation for 3 h. Although cysteine proteinase inhibitor E-64 was also effective in preventing protein degradation, inhibitors for metallo- and asparatic proteinases did not reveal obvious inhibitory effects. Our present results strongly suggested that the naturally occurring legume bean seed protein MBTI can be used as an effective additive in preventing marine fish blue scad surimi gel softening, which is quite possibly caused by myofibril-bound serine proteinase (MBSP).
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