9 research outputs found

    Characterization, Identification and Application of Acinetobacter baumannii Serdang 1 for Phenol Biodegradation

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    Phenolic compounds has long been recognized as one of the most recalcitrant and persistent substance .in petroleum refinery effluents. The potential of microorganisms to catabolize and metabolize aromatic compounds has been recognized as effective means of disposing the hazardous wastes. A locally isolated bacterial strain Serdang 1 was investigated for phenol degradation. Based on Biolog ™ Identification System and a BLASTN search of GenBank, the complete sequences of bacteria strain Serdang 1 shared 98% similarity with Acinetobacter baumannii. The bacteria strain Serdang 1 was redesignated Acinetobacter baumannii Serdang 1 and was deposited at the GenBank under the accession number EF525671

    Characterization, Identification and Application of Acinetobacter baumannii Serdang 1 for Phenol Biodegradation

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    Phenolic compounds has long been recognized as one of the most recalcitrant and persistent substance .in petroleum refinery effluents. The potential of microorganisms to catabolize and metabolize aromatic compounds has been recognized as effective means of disposing the hazardous wastes. A locally isolated bacterial strain Serdang 1 was investigated for phenol degradation. Based on Biolog ™ Identification System and a BLASTN search of GenBank, the complete sequences of bacteria strain Serdang 1 shared 98% similarity with Acinetobacter baumannii. The bacteria strain Serdang 1 was redesignated Acinetobacter baumannii Serdang 1 and was deposited at the GenBank under the accession number EF525671

    Characterization and identification of newly isolated Acinetobacter baumannii strain Serdang 1 for phenol removal

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    A new indigenous bacterial strain from Malaysian soil contaminated with petroleum waste had been successfully isolated, characterized and identified for phenol removal. The gram negative bacteria showed 98% identity with Acinetobacter baumannii based on Biolog™ Identification System and the determination of a partial 16S ribosomal RNA (rRNA) sequence. The isolate clustered with species belonging to Acinetobacter clade in a 16S rDNA-based neighbour-joining phylogenetic tree

    Phenol removal by newly isolated Acinetobacter baumannii strain Serdang 1 in a packed-bed column reactor

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    A newly isolated Acinetobacter baumannii strain Serdang 1 was explored for its potential in phenol remediation in batch and continuous system. An immobilization cell system has been successfully developed to remove phenol in a batch system as high as 2,000 mg/L in 12 d at a rate of 6.04 mg/L/h. Repeated use of immobilized cells as many as five cycles was shown without any loss of activity. The continuous system in a packed-bed reactor achieved 65–77% phenol removal at the rate of 38.4 mg/L/h for 200 mg/L influent, which was almost three fold higher than the batch system. Low influent flow rate at 1.5 mL/min and bed height-to-diameter ratio of 15.2 reached steady state faster than the higher flow rate, and the percentage of phenol removal was also higher

    Characterization of a molybdenum-reducing Acinetobacter baumannii strain Serdang 1 with the capacity to grow on phenol and acrylamide

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    Contamination of organic xenobiotic pollutants and heavy metals in a contaminated site allows the use of multiple bacterial degraders or bacteria with the ability to detoxify numerous toxicants at the same time. A previously isolated SDS- degrading bacterium, Acinetobacter baumannii strain Serdang 1 was shown to reduce molybdenum to molybdenum-blue. The bacterium works optimally at pH 6.5, the temperature range between 25 and 34°C with glucose serves as the best electron donor for molybdate reduction. This bacterium required additional concentration of phosphate at 5.0 mM and molybdate between 15 and 25 mM. The absorption spectrum of the molybdenum blue obtained is similar to the molybdenum blue from other earlier reported molybdate reducing bacteria, as it resembles a reduced phosphomolybdate closely. Ag(i), As(v), Pb(ii) and Cu(ii) inhibited molybdenum reduction by 57.3, 36.8, 27.7 and 10.9%, respectively, at 1 p.p.m. Acrylamide was efficiently shown to support molybdenum reduction at a lower efficiency than glucose. Phenol, acrylamide and propionamide could support the growth of this bacterium independently of molybdenum reduction. This bacterium capability to detoxify several toxicants is an important tool for bioremediation in the tropical region

    Tropomyosin and Actin Identified as Major Allergens of the Carpet Clam (Paphia textile) and the Effect of Cooking on Their Allergenicity

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    Objectives. To identify the major allergenic proteins of clam (Paphia textile) and to investigate the effect of different cooking methods on the allergenicity of these identified proteins. Methods. Clam protein extracts were separated by denaturing polyacrylamide gel electrophoresis. IgE reactive proteins were then analyzed by immunoblotting with sera from patients with positive skin prick tests (SPT) to the raw clam extract. Mass spectrometry was used to identify the major allergenic proteins of this clam. Results. Raw extract showed 12 protein bands (18–150 kDa). In contrast, fewer protein bands were seen in the boiled extract; those ranging from 40 to 150 kDa were denatured. The protein profiles were similarly altered by frying or roasting. The immunoblots of raw and boiled extracts yielded 10 and 2 IgE-binding proteins, respectively. The fried and roasted extracts showed only a single IgE-binding protein at 37 kDa. Mass spectrometry analysis of the 37 and 42 kDa major allergens indicated that these spots were tropomyosin and actin, respectively. Conclusion. The two major allergens of Paphia textile were identified as the thermostable tropomyosin and a new thermolabile allergen actin

    Identification of Major and Minor Allergens of Black Tiger Prawn ( Penaeus monodon ) and King Prawn ( Penaeus latisulcatus )

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    Background: Prawns and shrimp are a frequent cause of seafood allergy mediated by IgE antibodies. Penaeus monodon and Penaeus latisulcatus , commonly known as black tiger prawn and king prawn, respectively, are among the most frequently consumed prawns in Malaysia. The aim of thi s study was to identify the IgE-binding proteins of these 2 prawn species. Methods: Raw and boiled prawn extracts were prepared and then resolved by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). IgE-immunoblotting was then performed using sera from patients with positive skin prick tests to the raw prawn extracts. Results: SDS-PAGE analysis of the raw extracts of both prawn species revealed 23 protein bands; the boiled extracts yielded fewer protein bands. The bands in the range of 40 to 100 kDa were sensitive to heat and therefore were not found in the boiled extracts. Immunoblot of raw extracts of black tiger prawns and king prawns yielded 14 and 11 IgE-binding proteins, respectively, with molecular weights of between 15 and 200 kDa. Proteins at 36, 42, and 49 kDa were detected as the major allergens in both species of prawns. A protein of 75 kDa was also identified as a major allergen in black tiger prawns. Other potential allergens were also observed at various molecular masses. Conclusion: Proteins of 36, 42, and 49 kDa were identified as the major allergens of both species of prawns. The 36 and 42 kDa proteins are hypothesised to be tropomyosin and arginine kinase, respectively. A high molecular weight protein of 75 kDa was found to be an additional major allergen in black tiger prawns
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