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Articles by M.I.A. Karim
Total Records ( 6 ) for M.I.A. Karim
  S. Abd-Aziz , L.G.A. Ong , M.A. Hassan and M.I.A. Karim
  The aims of this study are to optimised the process parameters involved for submerged fermentation of mannanase by Aspergillus niger FTC5003 using palm kernel cake (PKC) as carbon source. The parameters investigated include temperature, agitation speed, inoculum size and PKC concentration. The submerged fermentation was carried out for 10 days by using palm kernel cake as the sole carbon source with the addition of nitrogen source. Palm kernel cake can be considered as a suitable carbon source for the enzyme production due to it mainly consist of mannan and galactomannan, which is hemicellulose. The mannanase enzyme production using the optimised fermentation condition, which was conducted at agitation speed of 200 rpm, temperature 35 °C, 1x104 spores mL-1 of inoculum size and 2% of palm kernel cake with productivity of 13.00 U/mL/day.
  N. Nadir , M. Mel , M.I.A. Karim and R.M. Yunus
  The two-step enzymatic hydrolysis of sweet sorghum and cassava were performed by commercially available α-amylase and glucoamylase and further ethanol fermentation of the obtained hydrolyzates by Saccharomyces cerevisiae were studied. For both sweet sorghum and cassava, the hydrolysis and fermentation were done in a 2 L stirred tank bioreactor, B-Braun fermenter, by using the same conditions. The amount of glucose obtained after hydrolysis process was greater in sweet sorghum compared to cassava, which are 50.07 and 40.00 g L-1, respectively. Also, sweet sorghum gave higher ethanol concentration than cassava at the 64 h of fermentation process, which are 40.11 and 34.07 g L-1, respectively.
  M. Mel , M.I.A. Karim and H.M. Salleh
  This study is focused on the evaluation of the volumetric mass transfer coefficient (kLa) of E. coli fermentation producing β-glucuronidase enzyme in different bioreactor operating conditions. The operating conditions used were according to the Taguchi’s method design using three factors of fermentation viz., temperature, agitation speed and air flow rate at two concentration levels. From the four experiments conducted, experimental run number two with agitation of 300 rpm, airflow rate of 2 vvm and temperature 41°C generate the highest Optical Density (OD 660 nm) of 2.313 for cell count and also having an equivalent kLa value of 0.0281 min-1 or 1.686 h-1. This condition was found to be an effective point for upscaling in bigger bioreactor for E. coli fermentation to produce the enzyme.
  R. Aloysius , M.I.A. Karim and A.B. Ariff
  Studies on the feasibility of using free and immobilized live cells of Rhizopus oligosporus as a biosorbent to remove cadmium from solution was carried out using shake flask experiments. The effect of various conditions such as pH, different initial cadmium concentrations, different biomass concentrations and initial cadmium concentration to biomass concentration ratio was investigated. The biosorption of Cd2+ was determined using several sorption isotherm models such as Langmuir and Scatchard plots. The Langmuir sorption model was found sufficient to describe the biosorption of cadmium by both immobilized and free cells, suggesting that the process was chemical, saturable and equilibrated mechanism similar to ion- exchange mechanism of metals adsorption. A curve of Scatchard transformation plot reflected the covalent nature of Cd2+ adsorption by live cells of Rhizopus oligosporus. Maximum uptake capacity for immobilized cells was about 2-fold higher (34.25 mg/g) than free cells. The immobilized cells projected a higher cadmium uptake capacity with increasing biomass concentration compared to free cells which reached optimum at 0.5 g/L. The initial cadmium concentration to biomass concentration ratio for immobilized cells was lower (33.3 mg/g) compared to free cells (200 mg/g) reflecting that effective removal of Cd2+ can be obtained with increasing immobilized biomass concentration. In bioreactor, the cadmium uptake capacity in comparison with shake flasks experiments for immobilized cells was not effected as observed for free cells. In fixed bed-column, packed-bed with immobilized cells permitted better process control with 2.5-fold higher (0.18 Lh–1) influent feeding rate achieved compared to packed-bed with free cells. About 99 per cent of cadmium removal was achieved for influent containing 5 mg/L and 20 mg/L of cadmium indicating strong affinity of free and immobilized live cells of Rhizopus oligosporus towards Cd2+.
  K.H. Kok , M.I.A. Karim , A.B. Ariff and S. Abd-Aziz
  Study on the feasibility of using Aspergillus flavus cells as biosorbent to remove lead from solution was carried out using a 500mL shake flask. The effect of metal concentration, biosorbent concentration, temperature and pH on lead adsorption were investigated. The maximum uptake of lead by Aspergillus flavus cells was 144.5 mg lead/g dry cell. The highest uptake of lead by this biosorbent was occurred at pH 4 and temperature 400C.
  Z. Shahrim , V. Sabaratnam , N.A.A. Rahman , S. Abd-Aziz , M.A. Hassan and M.I.A. Karim
  Trichoderma sp. KUPM0001 showed good growth during solid substrate fermentation (SSF) of sago pith residue known as hampas, supplemented with 10% (v/w) of mineral salts solution containing 0.5% (w/v) (83.3 mM) urea as nitrogen source and an initial moisture content of 80% (v/w). Mycelium suspension of 10% (v/w) density was used as initial inoculum and SSF was carried out at 25±2°C in static condition over a period of 120 h. The parameters optimized included the initial moisture content of the substrate, mineral salts solution, urea concentration, inoculum density, incubation temperature and incubation time. Without optimized condition, the maximum reducing sugar obtained was 24 mg mL-1 compared to 46 mg mL-1 substrate during optimized SSF after 96 h incubation. The optimum parameters obtained were 80% (v/w) of initial moisture; 10% (v/w) of inoculums size; 1.0% of urea in 20% (w/v) of mineral solution and incubated at 30±2°C. The enzyme activities using optimized condition gave maximum α-amylase, glucoamylase, carboxymethyl cellulase, filter paperase and β-glucosidase of 3.19, 2.22, 1.66, 1.11 and 1.48 U mL-1, respectively.
 
 
 
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