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Articles by Lubna Yasmin
Total Records ( 4 ) for Lubna Yasmin
  Moshiur Rahaman , Lubna Yasmin , Md. Kamal , M.A. Mazid and Md. Nazrul Islam
  The effect of delayed icing on the quality of ice-stored Brackish water shrimp (Penaeus monodon) was investigated by determining organoleptic, biochemical and bacteriological aspects. The live shrimp samples stored in ice immediately after harvest were organoleptically acceptable for 10 days while delay in icing for 4, 8 and 12 hrs shortened the shelf life to 7, 6 and 5 days, respectively. The initial pH of the live shrimp muscles was 6.63 which increased to 7.28 after 10 days of ice storage while in samples delayed in icing for 4, 8 and 12 h pH increased to 7.85, 7.93 and 7.95, respectively at the end of 10 days of ice storage. TVB-N value was increased from 5.88 to 32.76 mg/100g after 10 days of ice storage. The peroxide values in all the samples were lower than 8 meq/kg of oil upto 5 days of ice storage and then increased gradually with the lapse of storage period. The myofibrillar Ca2+-ATPase activity in presence of 0.5M KCl showed the maximum remaining activity of 0.52 μmol pi/ in live samples stored in ice immediately after catch. The myofibrillar solubility of samples immediately after catch was 80%, which decreased around 50% during 10 days of storage. On the other hand, the solubility of the samples kept at room temperature for different periods prior to icing were around 70% which decreased considerably to about 40% during 10 days of storage. The aerobic plate count (APC) increased considerably in the samples kept at ambient temperature for longer period prior to icing. The composition of bacteria in samples was Coryneforms (8.33%), Bacillus (7.40%), Micrococcus (16.66%), Achromobacter (8.33%), Flavobacterium/Cytophaga (25%), Pseudomonus (25%) and Vibrio (8.33%). Shrimp samples iced at 4,8 and 12 hrs delay dominated mostly by Micrococcus with 60%, 57.14% and 46.66%, respectively. During subsequent storage for 7 days, Micrococcus and Achromobacter were dominant in all the samples. However, Enterobacteriaceae was found in samples delayed 8 and 12 hr prior to icing.
  Md. Kamal , B.C. Biswas , Lubna Yasmin , K.M. Azimuddin and Md. Nazrul Islam
  Seven species of marine fish such as Queenfish (Chorinemus lysan), Jew fish (Otolithus argenteus), Silver belly (Leiognethus spp.), hard tail (Megalespis cordyla), lizard fish (Saurida tumbil), Bombay duck (Harpadon nehereus) and catfish (Tachyssurus thalassinnus) having limited use in fresh market were used in present study for evaluation of gel forming ability under a wide range of incubation temperature. The resulting suwari gels were subjected to the puncture test, expressible moisture test, teeth cutting test and folding test. The gel strength of Chorinemus lysan suwari-gel in one-step heating showed the maximum breaking force at 45°C (1196 ± 32g) after incubation for 120 minutes. In case of two-step heating, the product heated at 40°C for 120 min had the highest gel strength (1485 ± 79g). The gel strength of Otolithus argenteus in one-step heating showed the higher breaking force (BF) at 50°C (926 ± 34g) for 180 min, while in two steps heating, the highest gel-strength of 1451 ± 49g was obtained at 45°C after an incubation of 120 minute. In Megalespis cordyla both in one-step and two-step heating, maximum breaking force was obtained at incubation temperature of 45-50°C. The gel-strength of Leiognethus sp. in one step heating had highest breaking force at 50°C for 120 minutes (1010 ± 51g) and in two-step process the highest breaking force was obtained after pre-heating at 40°C for 180 min (1323 ± 58g). The results of gel strength Saurida tumbil suwari-gel both in one step and two-step heating showed poor ability irrespective of incubation temperature used. H. nehereus showed poor gel strength with maximum range of 207-213g at the temperature range of 40 -50°C both in one and two steps heating at various incubation temperatures. In T. thalassinus, the highest gel strength of 420 ± 87 g was obtained at 35°C in 180 minutes during one step heating while in two step heating, the resulting suwari-gel of T. thalassinus was the highest after pre-heating at 35°C for 120 min (313 ± 12 g).
  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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