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| Effect of Konjac Oligosaccharides on Myofibrillar Protein Gel Properties under Low-Salt Conditions |
| ZHENG Ruihan, CUI Bingbing, LI Ke, CHEN Bo, MA Wuchao, WU Haitao, YAN Jianan, BAI Yanhong |
| 1. Key Laboratory of Cold Chain Food Processing and Safety Control, Ministry of Education, College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450001, China; 2. National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China; 3. College of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China |
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Abstract This study aimed to investigate the effect of addition of different levels (0, 0.5, 1, 1.5, and 2 g/100 mL) of konjac oligosaccharides (KOS) on the gel properties of myofibrillar protein (MP) from chicken breast meat under low-salt conditions (0.3 mol/L NaCl). Changes in the gel properties of MP incorporated with different levels of KOS were evaluated by measurement of cooking loss, gel strength, rheological properties, water distribution, protein secondary structure, and intermolecular forces as well as microstructural observation. The results indicated that under low-salt conditions, compared with the control group (without added KOS), the addition of KOS improved the gel properties of MP and maintained the stability of the gel system. As the level of KOS addition increased from 0 to 2 g/100 mL, both the water-holding capacity and strength of gels initially increased and then decreased. Compared with the control group, the cooking loss of gels with added KOS at 1.5 g/100 mL significantly decreased to 22.73% (P < 0.05), while the gel strength significantly increased by 58.80% (P < 0.05). The storage modulus (G’) also showed a trend of first increasing and then decreasing, reaching its maximum at a KOS concentration of 1.5 g/100 mL. This indicates that KOS significantly enhanced the viscoelasticity of the MP gel system. Water distribution analysis demonstrated that at this KOS concentration, the proportion of immobilized water significantly increased, while that of free water significantly decreased (P < 0.05). Secondary structure analysis revealed that KOS addition promoted the transition from α-helix to β-sheet, facilitating the unfolding of protein molecules. Intermolecular force results indicated that the addition of 1.5 g/100 mL KOS resulted in the highest hydrophobic interaction and disulfide bond contents, significantly exceeding those of the control group (P < 0.05). Furthermore, scanning electron microscopy images showed that the gel network structure of the 1.5 g/100 mL KOS group was more compact with smaller pores. In conclusion, KOS can improve the properties of low-salt chicken MP gels, with the most pronounced effect observed at an addition level of 1.5 g/100 mL. This finding provides a basis for maintaining the stability of MP gel systems under low-salt conditions.
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2026, Vol. 40 
