Aim : 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.

Biodegradation of agricultural wastes, generated annually from poultry farms and slaughterhouses, can solve the pollution problem and at the same time yield valuable degradation products. But these wastes also constitute environmental nuisance, especially in Malaysia where their illegal disposal on heavy metal contaminated soils poses a serious biodegradation issue as feather tends to accumulate heavy metals from the surrounding environment. Further, continuous use of feather wastes as cheap biosorbent material for the removal of heavy metals from effluents has contributed to the rising amount of polluted feathers, which has necessitated the search for heavy metal-tolerant feather degrading strains. Isolation, characterization and application of a novel heavy metal-tolerant feather-degrading bacterium, identified by 16S RNA sequencing as Alcaligenes sp. AQ05-001 in degradation of heavy metal polluted recalcitrant agricultural wastes, have been reported. Physico-cultural conditions influencing its activities were studied using one-factor-at-a-time and a statistical optimisation approach. Complete degradation of 5 g/L feather was achieved with pH 8, 2% inoculum at 27 degrees C and incubation period of 36 h. The medium optimisation after the response surface methodology (RSM) resulted in a 10-fold increase in keratinase production (88.4 U/mL) over the initial 8.85 U/mL when supplemented with 0.5% (w/v) sucrose, 0.15% (w/v) ammonium bicarbonate, 03% (w/v) skim milk, and 0.01% (w/v) urea. Under optimum conditions, the bacterium was able to degrade heavy metal polluted feathers completely and produced valuable keratinase and protein-rich hydrolysates. About 83% of the feathers polluted with a mixture of highly toxic metals were degraded with high keratinase activities. The heavy metal tolerance ability of this bacterium can be harnessed not only in keratinase production but also in the bioremediation of heavy metal polluted feather wastes. (C) 2016 Published by Elsevier Ltd.

The characterization of bacterial enzymatic pathways of phenol metabolism is important to better understand phenol biodegradation. Phenol hydroxylase is the first enzyme involved in the oxidative metabolism of phenol, followed by further degradation via either meta-or ortho-pathways. In this study, the first known instance of phenol degradation via the meta-pathway by a member of the genus Acinetobacter (Acinetobacter sp. strain AQ5NOL 1) is reported. Phenol hydroxylase converts phenol to catechol, which is then converted via the meta-pathway to 2-hydroxymuconic semialdehyde by the catechol 2,3-dioxygenase enzyme. Phenol hydroxylase extracted from strain AQ5NOL 1 was fully purified using DEAE-Sepharose((R)), DEAE-Sephadex((R)), Q-Sepharose((R)) and Zorbax((R)) Bioseries GF-250 gel filtration and was demonstrated by SDS-PAGE to have a molecular weight of 50 kDa. The phenol hydroxylase was purified to about 210.51 fold. The optimum pH and temperature for enzyme activities are 20 degrees C and 7- 7.5, respectively. The apparent K-m and V-max values of phenol hydroxylase with phenol as the substrate were 13.4 mu M and 2.5 mu mol min(-1) mg(-1), respectively. The enzyme was stable at -20 degrees C for 36 days.

Gold mining companies are known to use cyanide to extract gold from minerals. The indiscriminate use of cyanide presents a major environmental issue. Serratia marcescens strain AQ07 was found to have cyanide-degrading ability. Optimisation of biodegradation condition was carried out utilising one factor at a time and response surface methodology. Cyanide degradation corresponded with growth rate with a maximum growth rate of 16.14 log cfu/mL on day 3 of incubation. Glucose and yeast extract are suitable carbon and nitrogen sources. Six parameters including carbon and nitrogen sources, pH, temperature, inoculum size and cyanide concentration were optimised. In line with the central composite design of response surface methodology, cyanide degradation was optimum at glucose concentration 5.5 g/L, yeast extract 0.55 g/L, pH 6, temperature 32.5 A degrees C, inoculum size 20 % and cyanide concentration 200 mg/L. It was able to stand cyanide toxicity of up to 700 mg/L, which makes it an important candidate for bioremediation of cyanide. The bacterium was observed to degrade 95.6 % of 200 mg/L KCN under the optimised condition. Bacteria are reported to degrade cyanide into ammonia, formamide or formate and carbon dioxide, which are less toxic by-products. These bacteria illustrate good cyanide degradation potential that can be harnessed in cyanide remediation.

The purpose of this study was to investigate the ability of Acinetobacter sp. strain AQ5NOL 1 immobilised in gellan gum beads to degrade phenol in the presence of heavy metals. Sewn different heavy metals, namely, As5+, Cu2+ Cd2+, Ni2+, Cr6+, Ph2+, and He at 1 ppm were tested. Results of the study showed that degradation of phenol by free cells was inhibited by Hg2+, Cu6+ and Cr6+ after 48 hours of incubation by 97.91 %, 77.58 % and 75.26 %, respectively. Only Hg2+ and Cr6+ inhibited phenol degradation by immobilised Acinetobacter cells in 18 hours by 67.55 % and 53.19 %. Phenol degradation by immobilised cells was affected when Cr and Hg2+ concentrations exceeded 0.5 and 0.1 ppm, respectively. However, inhibitory effects of heavy metals can be overcome by prolonging the incubation time for immobilised Acinetobacter sp. strain AQ5NOL 1 from 18 hours to 24 and 30 hours for Cr6+ (46.80 %) and Hg2+ (21.40 %), respectively.