ABSTRACT
Aims: Trichoderma asperellum strain SD1 grows on 3-chloropropionic acid (3CP), a β-haloalkanoic acid, and produces a putative extracellular dehalogenase that can degrade this acid. Here we further characterized the fungal enzyme system responsible for biodegradation of 3CP. Methodology and results: The primary qualification of the ligninolytic potential in T. asperellum strain SD1 was performed using guaiacol oxidation. When strain SD1 was grown in liquid minimal medium with the presence of 3CP as the sole carbon source, no lignin peroxidase, manganese peroxidase, or laccase activity was detected. The ligninolytic condition was achieved only in the presence of glucose or when guaiacol was present as an inducer. Under nonligninolytic conditions, 3CP was utilized by strain SD1. Therefore, 3CP was utilized under ligninolytic conditions as well as under non-ligninolytic conditions, suggesting that extracellular peroxidases and laccase are not involved in the degradation of 3CP by T. asperellum strain SD1. Conclusion, significance, and Impact of study: Very few studies have explained the degradation of β-chloro– substituted haloalkanoic acids such as 3CP by dehalogenases. This is the first report to identify a novel putative β- haloacid dehalogenase that degrades 3CP under ligninolytic and non-ligninolytic conditions. T. asperellum strain SD1, thus has the potential in the development of dehalogenating enzymes for industrial biocatalytic processes, in future.