Bacillus thuringiensis (Bt.) produces protein inclusions (parasporal inclusions) adjacent to the endospore during sporulation. The parasporal inclusions consist of one or more insecticidal proteins in the form of a crystal or crystal complex. These insecticidal proteins are commonly known as insecticidal crystal proteins (ICP) or delta (δ) endotoxin. The primary insecticidal activity of Bt. is due to ICP (Espinasse et al., 2002). It comprised of 90% of microbial insecticides produced in the world (Bajwa and Kogan, 2001). Bt. typically produces δ-endotoxins in parallel with spore formation during the stationary phase of the cell growth cycle (NPTN, 2004). The Cry1 proteins are a group of delta endotoxins that principally target lepidopteran species, including several important crop pests (Swadener, 1994). PCR screening for gene content of MPOB indigenous isolates showed that several of these isolates harbour toxins effective for oil palm lepidopteran pest (Ramlah Ali and Basri, 2002). In oil palm industry, defoliators such as bagworms, nettle caterpillars (Siti Ramlah et al., 2003) and bunch moth can be effectively controlled using Bt product (Mohd Basri et al., 1994; Siti Ramlah and Mohd Basri, 1997). Indigenous Bt. isolates containing the right Cry proteins and devoid of β-exotoxin can be propagated at pilot-scale as ideal alternative to chemical. The undesirable effect of chemical pesticides on the environment and biodiversity has create a niche for the use of environmentally safe alternative, the Bt.

Main Research: Dr Siti Ramlah Ahmad Ali