Nakamizo Ryoko, Hayashi Tatsuya, Kominami Yuri, Ushio Hideki
Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan.
Fish Protein Laboratory, Suzuhiro Kamaboko Honten Co., Ltd., Odawara 250-0862, Japan.
Gels. 2025 May 8;11(5):348. doi: 10.3390/gels11050348.
Surimi gel, a type of hydrocolloidal food, is formed through the gelation of fish meat proteins. Myosin heavy chain (MHC), a key myofibrillar protein, plays a crucial role in the formation of the gel network via both transglutaminase (TGase)-catalyzed and non-enzymatic polymerization. Gel disintegration in surimi is primarily attributed to the proteolytic degradation of MHC. This study focused on golden threadfin bream , a species characterized by low TGase activity and high protease activity at elevated temperatures. We investigated the competition between non-enzymatic polymerization and proteolytic degradation of MHC and their effects on gel mechanical properties using a mathematical model. A mathematical model based on kinetic reactions accurately reflected the changes in MHC observed through SDS-PAGE analysis during gel disintegration. Our results indicate that not only unpolymerized but also polymerized MHC was significantly degraded, which substantially contributed to the reduction in the mechanical properties of the surimi. Mathematically understanding the dynamics of MHC in surimi during heating helps promote the utilization of noncommercial fish species for surimi processing by enabling better control over surimi gel properties.
鱼糜凝胶是一种水胶体食品，它通过鱼肉蛋白的凝胶化形成。肌球蛋白重链（MHC）是一种关键的肌原纤维蛋白，在转谷氨酰胺酶（TGase）催化的和非酶促聚合过程中，对凝胶网络的形成起着至关重要的作用。鱼糜中的凝胶解体主要归因于MHC的蛋白水解降解。本研究聚焦于金线鲷，该物种在温度升高时具有低TGase活性和高蛋白酶活性的特点。我们使用数学模型研究了MHC的非酶促聚合与蛋白水解降解之间的竞争及其对凝胶力学性能的影响。基于动力学反应的数学模型准确反映了在凝胶解体过程中通过SDS - PAGE分析观察到MHC的变化。我们的结果表明，不仅未聚合的MHC，而且聚合的MHC也显著降解，这在很大程度上导致了鱼糜力学性能的降低。从数学上理解加热过程中鱼糜中MHC的动态变化，有助于通过更好地控制鱼糜凝胶特性，促进非商业鱼类物种在鱼糜加工中的利用。
