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Journal of Environmental Biology

pISSN: 0254-8704 ; eISSN: 2394-0379 ; CODEN: JEBIDP
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    Abstract - Issue May 2017, 38 (3)                                     Back


nstantaneous and historical temperature effects on a-pinene

Characterisation of cholinesterase from kidney tissue of Asian seabass (Lates calcarifer) and its inhibition in presence of metal ions

 

N. M. Hayat1, S. A. Ahmad1*, N. A. Shamaan2, M. K. Sabullah1,3, M. Y. A. Shukor1, M. A. Syed1, A. Khalid4,

K. A. Khalil5 and F. A. Dahalan6

1Department of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400, UPM Serdang, Selangor, Malaysia

2Faculty of Medicine and Health Sciences, Universiti Sains Islam Malaysia, 55100, Kuala Lumpur, Malaysia

3Faculty of Science and Natural Resource, Universiti Malaysia Sabah, 88400, Kota Kinabalu, Sabah, Malaysia

4Faculty of Health Sciences, Universiti Kebangsaan Malaysia, 50300, Kuala Lumpur, Malaysia

5Department of Biomolecular Sciences, Faculty of Applied Sciences, Universiti Teknologi MARA, 40150, Shah Alam, Selangor, Malaysia

6The School of Environmental Engineering, Universiti Malaysia Perlis, 02600, Arau, Perlis, Malaysia

*Corresponding Author E-mail: aqlima@upm.edu.my

 

 

 

Key words

Biomarker,

Cholinesterase,

Metal ions,

Lates calcarifer

 

 

 

Publication Data

Paper received : 21.03.2015

Revised received : 30.07.2016

Accepted : 13.09.2016

 

Abstract

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 (Km) and Vmax value obtained was 0.1426 mM and 0.0217 ?mol min-1mg-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?C in Tris-HCl 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. 

 

 

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