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Articles by M. Neazuddin
Total Records ( 3 ) for M. Neazuddin
  M.I. Hossain , M. Kamal , M.N. Sakib , F.H. Shikha , M. Neazuddin and M.N. Islam
  An investigation was carried out on the quality changes in surimi prepared from ice stored Queen fish (Chorinemus lysan) in time interval during 20 days of storage in ice storage condition and the ratio of the fish to ice was maintained 1:1. Mince was prepared in both washed and unwashed condition. To evaluate the gel-forming characteristics, a portion of the mince was washed with water containing 0.1% NaCl. Both washed and unwashed mince were ground with 3% NaCl for 20 min at 4°C. The ground paste was stuffed into polyethylene tube and incubated at various temperatures (40, 50 and 60°C) for 2 h. The quality changes during ice storage of mince prepared from the ice stored fish muscle were evaluated with time interval by determining the gel-forming ability, myofibrillar Ca2+-ATPase activity, protein solubility and pH value of fish muscle. The resulting gels were subjected to the puncture test, teeth cutting test and folding test. Maximum breaking force was obtained from both washed and unwashed mince at the incubation temperature of 50°C. The gel strength of both unwashed and washed meat paste gradually declined with lapse of storage period and washed meat paste showed higher gel forming ability than unwashed meat paste throughout the study period. Myofibrillar Ca2+-ATPase activity, protein solubility and pH of the ice stored muscles decreased from 0.847 to 0.309 μmol pi min 1 mg 1, 87 to 12% and 6.69 to 5.89, respectively, during 20 days of ice storage.
  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.
  M. Kamal , M. Ismail Hossain , M.N. Sakib , F.H. Shikha , M. Neazuddin , M.A.J. Bapary and M.N. Islam
  Studies were conducted to evaluate the effect of salt concentration on the gel forming ability of surimi prepared from Queen fish (Chorinemus lysan) using various concentration of salt (0, 1, 2, 3, 4, 5 and 6%) in meat paste. In both one step (50°C for 2 h) and two steps heating process (50°C for 2 h prior to heating at 80°C for 30 min), maximum gel-strength was obtained at the salt concentration of 3% NaCl. In order to investigate the effect of cryoprotectants on the gel-forming ability of surimi prepared from Queen fish (Chorinemus lysan) during 3 weeks frozen storage, different combination of sucrose, sorbitol and polyphosphate were used. In both one and two steps heating process, the highest gel-forming ability was obtained from combination of 4% sucrose + 4% sorbitol + 0.3% polyphosphate, indicating that above combination of cryoprotective agents during frozen storage is suitable for surimi prepared from Queen fish (C. lysan).
 
 
 
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