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| Protein Isolation and Characterization of the Adductor Muscle of Chlamys nobilis |
| ZHU Yahui1, CAO Wenhong1, 2,*, HAN Linsen1, ZHANG Chaohua1,2 |
1. College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China;
2.Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Key Laboratory of Advanced Processing of Aquatic Products of Guangdong Higher Education Institution, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Zhanjiang 524088, China |
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Abstract Adductor muscle is an important edible part of Chlamys nobilis which has been processed and exploited as a rich source of protein due to its delicious taste. In this paper, amino acid analysis, molecular weight distribution and thermal stability were investigated on adductor muscle protein from Chlamys nobilis. The results demonstrated that the contents of moisture and protein in adductor muscle from Chlamys nobilis were 78.12% and 18.19%, respectively. Three protein components were isolated from adductor muscle including myofibrillar protein, myostromin and myosinogen representing 46.80%, 32.70% and 20.5% of the total proteins, respectively. The analysis of amino acid composition indicated that a wide variety of amino acids were found in the three proteins with essential to total amino acid ratios of 41.52%, 38.96% and 35.49% for myosinogen, myofibrillar protein and myostromin, respectively. sodium dodecyl sulfate-polyacrylamide gelelectrophoresis (SDS-PAGE) analysis showed that the subunit molecular weights of myosinogen were in the range of 16 ～ 105 kD, those of myofibrillar protein mostly ranged from 35 to 50 kD and near 105 kD, and myostromin had two obvious bands between 35 and 50 kD and one band near 71 kD. Thermal stability analysis indicated that the denaturation temperature of myosinogen, myofibrillar protein, mystromin was 65.8, 50.5 and 59.6 ℃, respectively.
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