Journal of Environmental Biology

Evaluation of acetylcholinesterase source from fish, Tor tambroides

for detection of carbamate

Siti Aqlima Ahmad¹*,Mohd Khalizan Sabullah², Nor Aripin Shamaan³, Mohd Yunus Abd Shukor¹, Hussain Jirangon¹,

Ariff Khalid⁴ and Mohd Arif Syed¹

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

Selangor, Malaysia.

²Faculty of Science and Natural Resources, Universiti Malaysia Sabah, Jalan UMS, 88400 Kota Kinabalu, Sabah.

³Faculty of Medicine and Health Sciences, Universiti Sains Islam Malaysia, 13th Floor, Menara B, Persiaran MPAJ, Jalan Pandan Utama,

Pandan Indah, 55100 Kuala Lumpur, Malaysia.

⁴Faculty of Health Sciences,? Universiti Kebangsaan Malaysia, Jalan Raja Muda Abdul Aziz, 50300 Kuala Lumpur, Malaysia

*Corresponding Author E-mail: aqlima@upm.edu.my, aqlimaahmad@gmail.com

Publication Data

Paper received:

10 February 2015

Revised received:

29 August 2015

Accepted:

06 October 2015

Abstract

Acetylcholinesterase (AChE) from the brain tissue of local freshwater fish, Tor tambroides was isolated through affinity purification. Acetylthiocholine iodide (ATCi) was preferable synthetic substrate to purified AChE with highest maximal velocity (V_max) and lowest biomolecular constant (K_m) at 113.60 Umg^-1 and 0.0689 mM, respectively, with highest catalytic efficiency ratio (V_max/K_m) of 1648.77. The optimum pH was 7.5 with sodium phosphate buffer as medium, while optimal temperature was in the range of 25 to 35 ?C. Bendiocarp, carbofuran, carbaryl, methomyl and propoxur significantly lowered the AChE activity greater than 50%, and the IC50 value was estimated at inhibitor concentration of 0.0758, 0.0643, 0.0555, 0.0817 and 0.0538 ppm, respectively.   

 Key words

Acetylcholinesterase, Brain, Carbamate, Organophosphate, Tor tambroides

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