肉类研究
肉類研究
육류연구
Meat Research
2015年
10期
10-15
,共6页
祝亚辉%曹文红%韩林森%章超桦
祝亞輝%曹文紅%韓林森%章超樺
축아휘%조문홍%한림삼%장초화
华贵栉孔扇贝%闭壳肌%蛋白分离%氨基酸%十二烷基磺酸钠-聚丙烯酰胺凝胶电泳%差示扫描量热法
華貴櫛孔扇貝%閉殼肌%蛋白分離%氨基痠%十二烷基磺痠鈉-聚丙烯酰胺凝膠電泳%差示掃描量熱法
화귀즐공선패%폐각기%단백분리%안기산%십이완기광산납-취병희선알응효전영%차시소묘량열법
Chlamys nobilis%adductor muscle%protein separation%amino acid%sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)%differential scanning calorimetry (DSC)
以华贵栉孔扇贝为研究对象，对其闭壳肌蛋白组分进行分离，并对其氨基酸组成、分子质量分布和热稳定性进行检测分析。结果表明：新鲜华贵栉孔扇贝闭壳肌中水分、粗蛋白含量分别为78.12%、18.19%；蛋白组分分离得到3种组成蛋白，其中肌原纤维蛋白占总蛋白46.80%，基质蛋白占32.70%，肌浆蛋白占20.50%；氨基酸组成检测表明3种蛋白组分氨基酸种类齐全，肌浆蛋白、肌原纤维蛋白、基质蛋白中必需氨基酸占氨基酸总量的百分比分别达到41.52%、38.96%、35.49%；十二烷基磺酸钠-聚丙烯酰胺凝胶电泳分析显示：肌浆蛋白亚基分子质量在16～105 kD之间分布广泛；肌原纤维蛋白组分分子质量大多介于35～50 kD和105 kD附近；基质蛋白组分在35～50 kD之间有2条明显的条带，在71 kD附近也有一条带；热稳定性分析显示肌浆蛋白、肌原纤维蛋白、基质蛋白的变性温度分别为65.8、50.5、59.6℃。
以華貴櫛孔扇貝為研究對象，對其閉殼肌蛋白組分進行分離，併對其氨基痠組成、分子質量分佈和熱穩定性進行檢測分析。結果錶明：新鮮華貴櫛孔扇貝閉殼肌中水分、粗蛋白含量分彆為78.12%、18.19%；蛋白組分分離得到3種組成蛋白，其中肌原纖維蛋白佔總蛋白46.80%，基質蛋白佔32.70%，肌漿蛋白佔20.50%；氨基痠組成檢測錶明3種蛋白組分氨基痠種類齊全，肌漿蛋白、肌原纖維蛋白、基質蛋白中必需氨基痠佔氨基痠總量的百分比分彆達到41.52%、38.96%、35.49%；十二烷基磺痠鈉-聚丙烯酰胺凝膠電泳分析顯示：肌漿蛋白亞基分子質量在16～105 kD之間分佈廣汎；肌原纖維蛋白組分分子質量大多介于35～50 kD和105 kD附近；基質蛋白組分在35～50 kD之間有2條明顯的條帶，在71 kD附近也有一條帶；熱穩定性分析顯示肌漿蛋白、肌原纖維蛋白、基質蛋白的變性溫度分彆為65.8、50.5、59.6℃。
이화귀즐공선패위연구대상，대기폐각기단백조분진행분리，병대기안기산조성、분자질량분포화열은정성진행검측분석。결과표명：신선화귀즐공선패폐각기중수분、조단백함량분별위78.12%、18.19%；단백조분분리득도3충조성단백，기중기원섬유단백점총단백46.80%，기질단백점32.70%，기장단백점20.50%；안기산조성검측표명3충단백조분안기산충류제전，기장단백、기원섬유단백、기질단백중필수안기산점안기산총량적백분비분별체도41.52%、38.96%、35.49%；십이완기광산납-취병희선알응효전영분석현시：기장단백아기분자질량재16～105 kD지간분포엄범；기원섬유단백조분분자질량대다개우35～50 kD화105 kD부근；기질단백조분재35～50 kD지간유2조명현적조대，재71 kD부근야유일조대；열은정성분석현시기장단백、기원섬유단백、기질단백적변성온도분별위65.8、50.5、59.6℃。
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 fromChlamys nobilis. The results demonstrated that the contents of moisture and protein in adductor muscle fromChlamys 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.
