Abstract：The synergistic effects of temperature (19—31 ℃) and salinity (22—38) on activities of amylase and Na+ /K+-ATPase were studied in juvenile scallop Chlamys nobilis with shell length of (7 .52 ± 0 .12) mm by two-factor central composite design (CCD) and response surface methodology (RSM ) .There were significant linear and quadratic effects of temperature on the activities of amylase and Na + /K+-A T Pase ( P<0 .05) .The significant linear effect of salinity on the activity of Na + /K+-ATPase was found (P<0 .05) ,without significant linear effect of salinity on the activity of amylase (P>0 .05) ,and the significant quadratic effects of salinity on the activities of amylase and Na + /K+-ATPase were observed (P<0 .05) . There were significant synergistic effects of both temperature and salinity on the activity of amylase (P<0 .05) ,and no significant synergistic effects of both temperature and salinity on the activity of Na + /K+-ATPase were observed . The activities of amylase and Na+ /K+-ATPase were inhibited under high temperature and salinity ,with gradual decline in activities of amylase and Na + /K+-ATPase .A model equation about the relationship between the activities of amylase and Na + /K+-ATPase and the two factors was established by response surface methodology ,with the r2 as high as 0 .9815 in temperature and 0 .9582 in salinity , indicating that the satisfactory fitting capability of the model was practicably applied for prediction .The optimization of the reliable model revealed that the maximum activities of amylase (0 .4809 U/mg) and Na+ /K+-ATPase (0 .0382 U/mg) ,with the desirability value of 0 .910 ,were observed at the 2-factor combination of water temperature of 25 .60 ℃ and a salinity of 30 .67 .
收稿日期: 2015-05-25
引用本文:
钱佳慧,栗志民,陈树河. 温度和盐度对华贵栉孔扇贝幼贝淀粉酶和 Na + /K +-ATP 酶活性的联合效应[J]. , 2015, 34(5): 269-276.
QIAN Jiahui,LI Zhimin,CHEN Shuhe. Synergistic Effects of Temperature and Salinity on Activities of Amylase and Na+ /K+-ATPase in Juvenile Scallop Chlamys nobilis (Reeve). , 2015, 34(5): 269-276.
