[Objective] The research aimed to find the optimal condition of corn starch production in the laboratory and analyze the soaking effect.[Method] The orthogonal test was used to determine the suitable technological con...[Objective] The research aimed to find the optimal condition of corn starch production in the laboratory and analyze the soaking effect.[Method] The orthogonal test was used to determine the suitable technological condition.By the light microscope and the scanning electron microscope,the soaking effect was analyzed.[Result] The suitable soaking condition was:soaking time 48 h,soaking temperature 55 ℃ and SO2 concentration 0.2%.The microscopic analysis result was that the protein matrix was sufficiently decomposed in the suitable soaking condition.The soaking effect had the positive correlation with the decomposed degree of protein matrix.[Conclusion] The research provided the basis for the soaking technics research of corn starch in the laboratory.展开更多
For understanding the function of tonoplast protein in plant cell signal pathway, we have identified an integral protein kinase activity from the highly purified tonoplast isolated from maize ( Zea mays L.) root by...For understanding the function of tonoplast protein in plant cell signal pathway, we have identified an integral protein kinase activity from the highly purified tonoplast isolated from maize ( Zea mays L.) root by a new nonradioactive method in which a color labeled peptide was used as substrate. The protein kinase was Ca 2+ _dependent and CaM and phosphatidylserine_independent, like the calmodulin_like domain protein kinase (CDPK) in many plants. The optimal pH value and Ca 2+ concentration were 6.5 and 10 μmol/L, respectively. According to the optimal pH value and the effect of detergent, it could be inferred that the active site of this protein kinase is oriented toward the cytoplasm. Zn 2+ had no obvious effect on its activity, indicating that this protein kinase has no zinc_finger domain that exists in some mammalian protein kinases. At the same time, when tonoplast proteins were prephosphorylated in the presence of Ca 2+ and ATP, both the ATP_hydrolysis and the proton_transport activity of vacuolar H +_ATPase were stimulated. This stimulation could be reversed by an alkaline_phosphatase. These results indicate that a Ca 2+ _dependent protein kinase was located in the tonoplast, and a Ca 2+ _dependent phosphorylation, probably caused by this kinase, activated the vacuolar H +_ATPase activity. These results are helpful for further research on the function of CDPK in the course of signal transduction in plants.展开更多
文摘[Objective] The research aimed to find the optimal condition of corn starch production in the laboratory and analyze the soaking effect.[Method] The orthogonal test was used to determine the suitable technological condition.By the light microscope and the scanning electron microscope,the soaking effect was analyzed.[Result] The suitable soaking condition was:soaking time 48 h,soaking temperature 55 ℃ and SO2 concentration 0.2%.The microscopic analysis result was that the protein matrix was sufficiently decomposed in the suitable soaking condition.The soaking effect had the positive correlation with the decomposed degree of protein matrix.[Conclusion] The research provided the basis for the soaking technics research of corn starch in the laboratory.
文摘For understanding the function of tonoplast protein in plant cell signal pathway, we have identified an integral protein kinase activity from the highly purified tonoplast isolated from maize ( Zea mays L.) root by a new nonradioactive method in which a color labeled peptide was used as substrate. The protein kinase was Ca 2+ _dependent and CaM and phosphatidylserine_independent, like the calmodulin_like domain protein kinase (CDPK) in many plants. The optimal pH value and Ca 2+ concentration were 6.5 and 10 μmol/L, respectively. According to the optimal pH value and the effect of detergent, it could be inferred that the active site of this protein kinase is oriented toward the cytoplasm. Zn 2+ had no obvious effect on its activity, indicating that this protein kinase has no zinc_finger domain that exists in some mammalian protein kinases. At the same time, when tonoplast proteins were prephosphorylated in the presence of Ca 2+ and ATP, both the ATP_hydrolysis and the proton_transport activity of vacuolar H +_ATPase were stimulated. This stimulation could be reversed by an alkaline_phosphatase. These results indicate that a Ca 2+ _dependent protein kinase was located in the tonoplast, and a Ca 2+ _dependent phosphorylation, probably caused by this kinase, activated the vacuolar H +_ATPase activity. These results are helpful for further research on the function of CDPK in the course of signal transduction in plants.