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| Effect of L-Histidine on Structural Characteristics and in Vitro Digestibility of Myofibrillar Protein at Low and High Salt Concentrations |
| GUO Xiuyun, XU Shuangyi, CAO Siyu, ZHANG Yawei |
| 1.College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China; 2.College of Tourism and Cuisine · College of Food Science and Engineering, Yangzhou University, Yangzhou 225009, China |
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Abstract The effect of L-histidine (His) (0, 0.2, 0.4 g/100 mL) on the structural characteristics and in vitro digestibility of pork myofibrillar protein (MP) was studied at low (0.2 mol/L NaCl) and high (0.6 mol/L NaCl) salt concentrations. The results showed that addition of His caused the unfolding of MP and the transformation of its molecular conformation at both low and high salt concentrations. The content of α-helical structure decreased, accompanied by an increase in the contents of other secondary structures (β-sheet, β-turn, random coil). Meanwhile, addition of His caused the exposure of the buried hydrophobic groups, resulting in increased surface hydrophobicity of MP. In addition, the content of α-helical structure of MP decreased (P < 0.05), and the surface hydrophobicity increased (P < 0.05) with increasing His concentration. The results of in vitro digestion showed that the addition of His significantly improved the in vitro digestibility of MP (P < 0.05) and reduced the particle size of the enzymatic hydrolysate (P < 0.05) regardless of salt concentration. Therefore, it could be concluded that His addition caused the unfolding of MP structure, resulting in the exposure of more enzymatic cleavage sites, facilitating the enzymatic hydrolysis of MP by pepsin and trypsin, thus improving the digestibility of MP.
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2022, Vol. 36 
