Universiti Teknologi Malaysia’s (UTM) Faculty of Biosciences and Medical Engineering researchers, in investigating dehalogenase enzyme, have discovered halogenated compound-degrading bacteria.
Research on dehalogenase has received a great deal of attention, as the presence of the dehalogenase enzyme is crucial for the removal of halogen. This is particularly significant as the enzyme can remove halogen from herbicides such as Dalapon, Glyphosate and Buster, which are the main contributors to environmental pollution due to its recalcitrance to biodegradation.
The study conducted by the Faculty of Biosciences and Medical Engineering research team focused on the ability of dehalogenase to act on halide ion located at carbon no 3, known as 3-chloropropionic acid which is particularly resistant to dehalogenase attack.
Deputy Dean Academic, Faculty of Biosciences and Medical Engineering, UTM Skudai, Assoc. Professor Dr Fahrul Zaman Huyop who led the research team stated that the discovery was based on several studies conducted by his research members related to dehalogenase enzyme.
From the study, chlorinated chemicals which hardly degrade in the environment, now appear to serve as a carbon source for certain microorganisms to support their growth.
This discovery is useful because it can overcome the current pollution problem through bioremediation process which is much safer for the environment.
“The present study focuses on the structure and function of dehalogenase from Rhizobium sp. using in silico technique and site-directed mutagenesis” Dr Fahrul clarified.
The study is conducted in collaboration with Dr Roswanira Ab Wahab, a protein chemist who helps to understand the basic mechanism of enzyme action.
In silico studies is applied to determine the stereospecificity of the enzyme. It involves performance on a computer or via computer simulation to analyze the structure and function of protein.
Site-directed mutagenesis is used to mutate current dehalogenase isolated from Rhizobium sp RC1 so that it can act on 3-chloropropionic acid, the substrate to which it was resistant before. This study was conducted by one of Dr Fahrul’s doctoral students.
Site-directed mutagenesis is a method to make specific and intentional changes to the DNA sequence of a gene. Hence, the specific sequence elements responsible for interactions involved in a cellular function can be identified. Additionally, site-directed mutagenesis can also be used to alter enzymes’ specificities. For instance, an enzyme which is originally stereospecific in nature, can be changed to non-stereospecific.
“Future research would involve crystallizing the protein. This step will aid in answering questions related to the in silico investigation,” Dr Fahrul added.