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Articles by Md. Moshiur Rahman
Total Records ( 2 ) for Md. Moshiur Rahman
  M.A.J. Bapary , Lubna Yasmin , Md. Moshiur Rahman , M. Neazuddin and Md. Kamal
  The influence of temperature on the changes in Ca2+-ATPase activity and solubility of M. rosenbergii and P. monodon muscle myofibrils were studied in a wide range of temperature from 20 to 55 ° C for 30 min. Both ATPase activity and solubility almost remain unchanged up to 25 ° C while both ATPase activity and solubility decreased with the raise of temperature. The decreasing of ATPase activity and solubility after 25 ° C clearly indicates the influence of temperature on the denaturation of M. rosenbergii muscle myofibrils. The influence of temperature on the inactivation rate of Ca2+-ATPase at 30 and 35 ° C on myofibrillar proteins of M. rosenbergii and P. monodon were investigated at various pH values. The inactivation rate of M. rosenbergii was low at pH 7.8 to 8.5 where the rate was quite high both in acidic and alkaline pH region irrespective of incubation temperature. The Kd value at 35 ° C was markedly higher than at 30 ° C throughout all the pH ranges. Similar studies were also conducted on P. monodon muscle myofibrils. The results obtained from P. monodon muscle myofibrils were more or less similar to that of Kd value obtained from M. rosenbergii muscle myofibrils where the myofibrils were found more stable at neutral pH ranges form 7.1 to 8.8. However, with the progress of acidic and alkaline pH value the Kd value gradually increased. The result also shows that higher temperature of 35 ° C accelerated the Kd value in myofibrils compared to that of incubated at 30 ° C throughout the pH ranges used.. Studies were also conducted to evaluate the effect of temperature on the coagulation time of sarcoplasmic protein of M.rosenbergii and P. monodon. At 40 ° C coagulation of M. rosenbergii sarcoplasmic protein was started in 8 min and coagulation time decreased gradually with the increase of temperature and at 60 ° C the coagulation of sarcoplasmic protein was started in 3 min. On the other hand, at 40 ° C coagulation of P. monodon sarcoplasmic protein started in 5 min and the coagulation time decreased with the raise of incubation temperature and it was found that at 60 ° C, coagulation was started within 1.7 min. The results obtained from present studies also shows that sarcoplasmic protein of P. monodon denature more quickly than that of M. rosenbergii sarcoplasmic protein at higher temperature.
  Md. Kamal , Md. Moshiur Rahman , Mohammad Abu Jafor Bapary , Lubna Yasmin and Md. Nurullah
  The influence of pH on the changes in myofibrillar remaining ATPase activities of M. rosenbergii and P. monodon was studied after storage at -20°C for 2 days, 0°C for 2 days and 35°C for 30 min. In all the three storage conditions, ATPase activities for both samples were lower in acidic and alkaline pH regions and the activity remains relatively high of 0.403 ° mol Pi/min mg at pH 8.1. The influence of pH on the remaining Mg2+-ATPase activity and Ca-sensitivity of M. rosenbergii and P. monodon were evaluated after storage at 0°C for 2 days and -20°C for 2 days. Mg2+-ATPase activities both in presence and absence of Ca2+ remain high at neutral pH compared to those of acidic and alkaline region. Ca-sensitivity were also very high (about 38 to 50% at pH ranges from 7.4 to 8.3) in neutral pH region where the sensitivity declined sharply both in acidic and alkaline pH region. The influence of pH on the changes in solubility of M. rosenbergii muscle myofibrils during ice and frozen storage was investigated. The highest solubility of 83 to 84% was obtained from myofibrils in the range of pH 7.4 to pH 7.9 after storage for 2 days in ice and -20°C for 2 days in frozen storage. The solubility decreased gradually both in acidic and alkaline pH regions. In the case of P. monodon, the maximum solubility of 84% were obtained at pH 7.9 after 2 days of storage at 0°C. Similarly the maximum solubility of 79% were obtained at same pH of 7.8 in myofibrils after storage at -20°C for 2 days. The solubility of P. monodon myofibrils was quite high in a wide range of pH from 6.8 to 8.3 and the solubility decreased gradually outside of these pH ranges. Comparatively higher solubility of 84% in a wide range of pH in myofibrils stored at 0°C compared to that of frozen storage also indicates the combined effect of pH and frozen storage on the denaturation of muscle myofibrils.
 
 
 
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