Underlying the mechanisms of incorporation of κ-carrageenan on the formation of low-salt myofibrillar protein gels during heating process: Perspective on the dynamic changes of protein structures and molecular interactions

被引:13
作者
Cao, Chuanai [1 ]
Zhang, Jingming [1 ]
Kong, Baohua [1 ]
Sun, Fangda [1 ]
Zhang, Hongwei [1 ]
Liu, Qian [1 ,2 ]
机构
[1] Northeast Agr Univ, Coll Food Sci, Harbin 150030, Heilongjiang, Peoples R China
[2] Heilongjiang Green Food Sci & Res Inst, Harbin 150028, Heilongjiang, Peoples R China
关键词
Low-salt myofibrillar protein; kappa-carrageenan; Gelation; Rheological behavior; Conformational; Intermolecular interactions; THERMAL GELLING PROPERTIES; GELATION PROPERTIES; MYOSIN; CONFORMATION; SURIMI; FISH; NACL;
D O I
10.1016/j.foodhyd.2024.110205
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
This study aimed to systematacially investigate the effects of kappa-carrageenan (KC) concentration on the formation of myofibrillar protein (MP) gels under low-salt condition based on the dynamic changes of protein structures and molecular interactions during heating process. The results indicated that incorporating KC markedly improved the water holding capacity (WHC) and gel strength of MP gels (P < 0.05). Those properties were most improved by adding 0.4% KC with WHC of 71.44% and gel strength of 1.62 N. During the heating process, when the temperature was above 50 degrees C, KC addition significantly increased the turbidity and particle size and decreased solubility of MP in a concentration-dependent manner, as well as exhibiting higher surface hydrophobicity at 0.2% KC concentration (P < 0.05), indicating that KC accelerated the rate of aggregation of MP during heating process. The dynamic rheological behaviors indicated that the addition of KC promoted the early unfolding and aggregation of MP at a relatively lower temperature, which was verified by the fluorescence denaturation mechanism results. Moreover, the addition of KC significantly promoted the heat-induced conformational transition of MP from alpha-helix companied with beta-sheet and beta-turn, which was due to the interaction between MP and KC accelerating the formation of MP gels during the heating process. Intermolecular forces results revealed that the aggregation of myosin head and cross-linking of myosin tail of MP added KC was enhanced by ionic bonds, hydrophobic interactions, and disulfide bonds, which facilitated the better gel performance. Our present results provided a comprehensive understanding of gelation mechanism of MP-KC mixed gels under low-salt condition, with implications for the practical application of KC in meat processing.
引用
收藏
页数:13
相关论文
共 58 条
  • [21] Mechanisms of inulin addition affecting the properties of chicken myofibrillar protein gel
    Han, Keying
    Li, Shanshan
    Yang, Yuling
    Feng, Xiao
    Tang, Xiaozhi
    Chen, Yumin
    [J]. FOOD HYDROCOLLOIDS, 2022, 131
  • [22] Study on the mechanism of mulberry polyphenols inhibiting oxidation of beef myofibrillar protein
    Huang, Xiang
    Sun, Lu
    Liu, Lan
    Wang, Guoze
    Luo, Peng
    Tang, Daobang
    Huang, Qun
    [J]. FOOD CHEMISTRY, 2022, 372
  • [23] Improved effect of flaxseed gum on the weakened gelling properties of myofibrillar protein induced by catechin
    Jia, Na
    Lin, Shiwen
    Zhang, Fengxue
    Zheng, Duoduo
    Liu, Dengyong
    [J]. FOOD CHEMISTRY, 2022, 372
  • [24] Effects of Mesona chinensis polysaccharide on the thermostability, gelling properties, and molecular forces of whey protein isolate gels
    Jiang, Lian
    Ren, Yanming
    Xiao, Yuehuan
    Liu, Shanshan
    Zhang, Jiahui
    Yu, Qiang
    Chen, Yi
    Xie, Jianhua
    [J]. CARBOHYDRATE POLYMERS, 2020, 242
  • [25] Thermal gelling properties and structural properties of myofibrillar protein including thermo-reversible and thermo-irreversible curdlan gels
    Jiang, Shuai
    Zhao, Shenchi
    Jia, Xiwen
    Wang, Hui
    Zhang, Huan
    Liu, Qian
    Kong, Baohua
    [J]. FOOD CHEMISTRY, 2020, 311
  • [26] Gelation properties of tilapia fish protein isolate and surimi pre- and post-rigor Rigor condition of tilapia FPI and surimi
    Kobayashi, Yuka
    Mayer, Steven G.
    Park, Jae W.
    [J]. FOOD BIOSCIENCE, 2017, 17 : 17 - 23
  • [27] Effect of konjac glucomannan on gelling and digestive properties of myofibrillar protein in Litopenaeus vannamei based on molecular docking
    Li, Deyang
    Li, Na
    Wang, Yefan
    Zhang, Kexin
    Tan, Zhifeng
    Liu, Huilin
    Liu, Xiaoyang
    Wu, Qiong
    Zhou, Dayong
    [J]. FOOD HYDROCOLLOIDS, 2024, 149
  • [28] Mechanism for improving the gel properties of transglutaminase-mediated porcine myofibrillar protein by ultrasonic pretreatment combined with carrageenan
    Li, Jihong
    Zhou, Yajun
    Li, Zongping
    Ma, Zhiyuan
    Ma, Qingshu
    Wang, Lu
    [J]. FOOD CHEMISTRY, 2023, 426
  • [29] Molecular forces and gelling properties of heat-set whole chicken egg protein gel as affected by NaCl or pH
    Li, Junhua
    Zhang, Mengqi
    Chang, Cuihua
    Gu, Luping
    Peng, Ning
    Su, Yujie
    Yang, Yanjun
    [J]. FOOD CHEMISTRY, 2018, 261 : 36 - 41
  • [30] Conformational and charge changes induced by L-Arginine and L-lysine increase the solubility of chicken myosin
    Li, Shiyi
    Li, Linxian
    Zhu, Xiaoxu
    Ning, Cheng
    Cai, Kezhou
    Zhou, Cunliu
    [J]. FOOD HYDROCOLLOIDS, 2019, 89 : 330 - 336