Jang Ho Sik, Lee Hong Chul, Chin Koo Bok
Department of Animal Science, Chonnam National University, Gwangju 61186, Korea.
Department of Animal Science, California Polytechnic State University, San Luis Obispo, CA 93407, USA.
Korean J Food Sci Anim Resour. 2016 Oct 31;36(5):671-678. doi: 10.5851/kosfa.2016.36.5.671.
Fractioning and/or preheating treatment on the rheological properties of myofibrillar protein (MP) gels induced by microbial transglutaminase (MTG) has been reported that they may improve the functional properties. However, the optimum condition was varied depending on the experimental factors. This study was to evaluate the effect of red bean protein isolate (RBPI) on the rheological properties of MP gels mediated by MTG as affected by modifications (fractioning: 7S-globulin of RBPI and/or preheat treatment (pre-heating; 95℃/30 min): pre-heating RBPI or pre-heating/7S-globulin). Cooking yields (CY, %) of MP gels was increased with RBPI (<0.05), while 7S-globulin decreased the effect of RBPI (<0.05); however, preheating treatments did not affect the CY (>0.05). Gel strength of MP was decreased when RBPI or 7S-globulin added, while preheat treatments compensated for the negative effects of those in MP. This effect was entirely reversed by MTG treatment. Although the major band of RBPI disappeared, the preheated 7S globulin band was remained. In scanning electron microscopic (SEM) technique, the appearance of more cross-linked structures were observed when RBPI was prepared with preheating at 95℃ to improve the protein-protein interaction during gel setting of MP mixtures. Thus, the effects of RBPI and 7S-globulin as a substrate, and water and meat binder for MTG-mediated MP gels were confirmed to improve the rheological properties. However, preheat treatment of RBPI should be optimized.
据报道，对微生物转谷氨酰胺酶（MTG）诱导的肌原纤维蛋白（MP）凝胶的流变学特性进行分级和/或预热处理可能会改善其功能特性。然而，最佳条件会因实验因素而有所不同。本研究旨在评估红豆分离蛋白（RBPI）对MTG介导的MP凝胶流变学特性的影响，该影响受改性（分级：RBPI的7S球蛋白和/或预热处理（预热；95℃/30分钟）：预热RBPI或预热/7S球蛋白）的影响。MP凝胶的烹饪产量（CY，%）随着RBPI的添加而增加（<0.05），而7S球蛋白降低了RBPI的影响（<0.05）；然而，预热处理对CY没有影响（>0.05）。添加RBPI或7S球蛋白时，MP的凝胶强度降低，而预热处理补偿了它们对MP的负面影响。MTG处理完全逆转了这种影响。尽管RBPI的主要条带消失了，但预热的7S球蛋白条带仍然存在。在扫描电子显微镜（SEM）技术中，当在95℃预热条件下制备RBPI时，观察到更多交联结构的出现，以改善MP混合物凝胶形成过程中的蛋白质-蛋白质相互作用。因此，证实了RBPI和7S球蛋白作为MTG介导的MP凝胶的底物、水和肉类粘合剂的作用，可改善流变学特性。然而，RBPI的预热处理应进行优化。
