Browsing by Author "Shukor, MYA"
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Publication Characterisation of cholinesterase from kidney tissue of Asian sea bass (Lates calcarifer) and its inhibition in presence of metal ions(Triveni Enterprises, 2017) ;Hayat, NM ;Ahmad, SA ;Shamaan, NA ;Sabullah, MK ;Shukor, MYA ;Syed, MA ;Khalid, A ;Khalil, KADahalan, FAAim : The cholinesterase (ChE) based inhibition studies from fish were investigated and presented here emerged to be one of the great potential biomarkers for heavy metals monitoring. Methodology : In this study, the capability of ChE extracted from the kidney of Lates calcarifer was assessed for of metal. ChE was purified through ammonium sulphate precipitation and ion exchange chromatography. Results : The purified enzyme gave 12 fold purification with the recovery of 12.17% with specific activity of 2.889 U mg(-1). The Michaelis-Menten constant (K-m) and V-max value obtained was 0.1426 mM and 0.0217 mu mol min(-1)mg(-1), respectively. The enzyme has the ability to hydrolyse acetylthiocholine iodide (ATC) at a faster rate compared to other two synthetic substrates, propionylthiocholine iodide (PTC) and butyrylthiocholine iodide (BTC). ChE gave highest activity at 20-30 degrees C in Tris-HCI buffer pH 8.0. The results showed that cholinesterase from L. calcarifer kidney was very sensitive to sensitive to copper and lead after being tested argentum, arsenic, cadmium, chromium, copper, cobalt, mercury, nickel, lead and zinc. Interpretation : The effect of heavy metals studied on the activity of ChE differed from each other. The result of the study can be used as a tool for further developing a biomarker for the detection of heavy metals in aquatic ecosystems. In addition, the information can also be used for designing a kit, that would give a rapid and accurate result. - Some of the metrics are blocked by yourconsent settings
Publication Enhanced phenol degradation by immobilized Acinetobacter sp strain AQ5NOL 1(Springer, 2012) ;Ahmad, SA ;Shamaan, NA ;Arif, NM ;Koon, GB ;Shukor, MYASyed, MAA locally isolated Acinetobacter sp. Strain AQ5NOL 1 was encapsulated in gellan gum and its ability to degrade phenol was compared with the free cells. Optimal phenol degradation was achieved at gellan gum concentration of 0.75% (w/v), bead size of 3 mm diameter (estimated surface area of 28.26 mm(2)) and bead number of 300 per 100 ml medium. At phenol concentration of 100 mg l(-1), both free and immobilized bacteria exhibited similar rates of phenol degradation but at higher phenol concentrations, the immobilized bacteria exhibited a higher rate of degradation of phenol. The immobilized cells completely degrade phenol within 108, 216 and 240 h at 1,100, 1,500 and 1,900 mg l(-1) phenol, respectively, whereas free cells took 240 h to completely degrade phenol at 1,100 mg l(-1). However, the free cells were unable to completely degrade phenol at higher concentrations. Overall, the rates of phenol degradation by both immobilized and free bacteria decreased gradually as the phenol concentration was increased. The immobilized cells showed no loss in phenol degrading activity after being used repeatedly for 45 cycles of 18 h cycle. However, phenol degrading activity of the immobilized bacteria experienced 10 and 38% losses after the 46 and 47th cycles, respectively. The study has shown an increased efficiency of phenol degradation when the cells are encapsulated in gellan gum.