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Hamid Reza Fard Masoumi,Mahiran Basri,Anuar Kassim,Dzulkefly Kuang Abdullah,Yadollah Abdollahi,Siti Salwa Abd Gani,Malahat Rezaee 한국공업화학회 2014 Journal of Industrial and Engineering Chemistry Vol.20 No.4
A wavelet neural network (WNN) based on the genetic algorithm (GA) was used in conjunction with an experimental design to optimize the enzymatic reaction conditions for the preparation of esteramines-based esterquats. A set of experiments was designed by central composite design to process modeling and statistically evaluate the findings. Five independent process variables, including enzyme amount, reaction time, reaction temperature, substrates molar ratio and agitation speed were studied under the given conditions designed by Design Expert software. All these show that the WNN has great potential ability in prediction of reaction conversion in lipase-catalyzed synthesis of products.
Optimization of Operational Conditions for Adipate Ester Synthesis in a Stirred Tank Reactor
Naz Chaibakhsh,Mohd Basyaruddin Abdul Rahman,Mahiran Basri,Farzaneh Vahabzadeh,Suraini Abd-Aziz,Abu Bakar Salleh 한국생물공학회 2010 Biotechnology and Bioprocess Engineering Vol.15 No.5
Esterification of adipic acid and oleyl alcohol in a solvent-free system featuring a stirred tank reactor containing commercially immobilized Candida antarctica lipase B was performed. The process was carried out using an artificial neural network (ANN) trained by the Levenberg-Marquardt (LM) algorithm. The effects of four operative variables, temperature, time, amount of enzyme,and impeller speed, on the reaction yield were studied. By examining different ANN configurations, the best network was found to consist of seven hidden nodes using a hyperbolic tangent sigmoid transfer function. The values of the coefficient of determination (R2) and root mean squared error (RMSE) between the actual and predicted responses were determined to be 1 and 0.0058178 for training and 0.99467 and 0.622540 for the testing datasets,respectively. These results imply that the developed model was capable of predicting the esterification yield. The operative variables affected the yield, and their order of contribution was as follows: time > amount of enzyme >temperature > impeller speed. A high percentage of yield (95.7%) was obtained using a low level of enzyme (2.5%w/w), and the temperature, time, and impeller speed were 66.5°C, 354 min (about 6 h), and 500 rpm, respectively. A simple protocol for efficient substrate conversion in a solvent-free system evidenced by high enzyme stability is indicative of successful ester synthesis.
Biodegradation of Hydrocarbon Contamination by Immobilized Bacterial Cells
Raja Noor Zaliha Abd. Rahman,Farinazleen Mohamad Ghazali,Abu Bakar Salleh,Mahiran Basri 한국미생물학회 2006 The journal of microbiology Vol.44 No.3
This study examined the capacity of immobilized bacteria to degrade petroleum hydrocarbons. A mixture of hydrocarbon-degrading bacterial strains was immobilized in alginate and incubated in crude oil-contaminated artificial seawater (ASW). Analysis of hydrocarbon residues following a 30-day incubation period demonstrated that the biodegradation capacity of the microorganisms was not compromised by the immobilization. Removal of n-alkanes was similar in immobilized cells and control cells. To test reusability, the immobilized bacteria were incubated for sequential increments of 30 days. No decline in biodegradation capacity of the immobilized consortium of bacterial cells was noted over its repeated use. We conclude that immobilized hydrocarbon-degrading bacteria represent a promising application in the bioremediation of hydrocarbon-contaminated areas.
S5 Lipase : An Organic Solvent Tolerant Enzyme
Raja Noor Zaliha Raja Abdul Rahman,Syarul Nataqain Baharum,Mahiran Basri 한국미생물학회 2006 The journal of microbiology Vol.44 No.6
In this study, an organic solvent tolerant bacterial strain was isolated. This strain was identified as Pseudomonas sp. strain S5, and was shown to degrade BTEX (Benzene, Toluene, Ethyl-Benzene, and Xylene). Strain S5 generates an organic solvent-tolerant lipase in the late logarithmic phase of growth. Maximum lipase production was exhibited when peptone was utilized as the sole nitrogen source. Addition of any of the selected carbon sources to the medium resulted in a significant reduction of enzyme production. Lower lipase generation was noted when an inorganic nitrogen source was used as the sole nitrogen source. This bacterium hydrolyzed all tested triglycerides and the highest levels of production were observed when olive oil was used as a natural triglyceride. Basal medium containing Tween 60 enhanced lipase production to the most significant degree. The absence of magnesium ions (Mg2+) in the basal medium was also shown to stimulate lipase production. Meanwhile, an alkaline earth metal ion, Na+, was found to stimulate the production of S5 lipase.
S5 Lipase : An Organic Solvent Tolerant Enzyme
Zaliha Raja Noor,Rahman Raja Abdul,Baharum Syarul Nataqain,Salleh Abu Bakar,Basri Mahiran The Microbiological Society of Korea 2006 The journal of microbiology Vol.44 No.6
In this study, an organic solvent tolerant bacterial strain was isolated. This strain was identified as Pseudomonas sp. strain S5, and was shown to degrade BTEX (Benzene, Toluene, Ethyl-Benzene, and Xylene). Strain S5 generates an organic solvent-tolerant lipase in the late logarithmic phase of growth. Maximum lipase production was exhibited when peptone was utilized as the sole nitrogen source. Addition of any of the selected carbon sources to the medium resulted in a significant reduction of enzyme production. Lower lipase generation was noted when an inorganic nitrogen source was used as the sole nitrogen source. This bacterium hydrolyzed all tested triglycerides and the highest levels of pro-duction were observed when olive oil was used as a natural triglyceride. Basal medium containing Tween 60 enhanced lipase production to the most significant degree. The absence of magnesium ions ($Mg^{2+}$) in the basal medium was also shown to stimulate lipase production. Meanwhile, an alkaline earth metal ion, $Na^+$, was found to stimulate the production of S5 lipase.
Biodegradation of Hydrocarbon Contamination by Immobilized Bacterial Cells
Rahman Raja Noor Zaliha Abd.,Ghazali Farinazleen Mohamad,Salleh Abu Bakar,Basri Mahiran The Microbiological Society of Korea 2006 The journal of microbiology Vol.44 No.3
This study examined the capacity of immobilized bacteria to degrade petroleum hydrocarbons. A mixture of hydrocarbon-degrading bacterial strains was immobilized in alginate and incubated in crude oil-contaminated artificial seawater (ASW). Analysis of hydrocarbon residues following a 30-day incubation period demonstrated that the biodegradation capacity of the microorganisms was not compromised by the immobilization. Removal of n-alkanes was similar in immobilized cells and control cells. To test reusability, the immobilized bacteria were incubated for sequential increments of 30 days. No decline in biodegradation capacity of the immobilized consortium of bacterial cells was noted over its repeated use. We conclude that immobilized hydrocarbon-degrading bacteria represent a promising application in the bioremediation of hydrocarbon-contaminated areas.
( Rahman ),( Raja Noor Zaliha Raja Abd ),( Noor Dina Muhd Noor ),( Noor Azlina Ibrahim ),( Abu Bakar Salleh ),( Mahiran Basri ) 한국미생물 · 생명공학회 2012 Journal of microbiology and biotechnology Vol.22 No.1
A thermophilic Bacillus stearothermophilus F1 produces an extremely thermostable serine protease. The F1 protease sequence was used to predict its three-dimensional (3D) structure to provide better insights into the relationship between the protein structure and biological function and to identify opportunities for protein engineering. The final model was evaluated to ensure its accuracy using three independent methods: Procheck, Verify3D, and Errat. The predicted 3D structure of F1 protease was compared with the crystal structure of serine proteases from mesophilic bacteria and archaea, and led to the identification of features that were related to protein stabilization. Higher thermostability correlated with an increased number of residues that were involved in ion pairs or networks of ion pairs. Therefore, the mutants W200R and D58S were designed using site-directed mutagenesis to investigate F1 protease stability. The effects of addition and disruption of ion pair networks on the activity and various stabilities of mutant F1 proteases were compared with those of the wild-type F1 protease.