• Journal of the Korean Wood Science and Technology
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• 제50권6호
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• pp.458-474
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• 2022

Many methods have been explored to increase the palatability of pine (Pinus merkusii), the most common wood used for termite baiting. However, because of the undersupply of pine in Indonesia, it is crucial to vary the wood species for termite baiting and look for potential alternatives. Furthermore, various studies have shown that baiting time influences the intensity and pattern of termite attacks. Therefore, the present research aimed to study the preferences of subterranean termites and find the ideal baiting time among community wood species from Bogor, West Java, as a baiting alternative to pine. The woods tested were Acacia mangium (acacia), Falcataria moluccana (sengon), Anthocephalus cadamba (jabon), Maesopsis eminii (manii), Swietenia mahagoni (mahogany), Hevea brasiliensis (rubberwood), and P. merkusii (pine). Field tests were carried out based on the American Society for Testing and Materials D 1758-06 at the Arboretum, Faculty of Forestry and Environment, IPB University, with a baiting time of one to six months. The results led to the identification of four species of termites, namely Microtermes sp., Macrotermes sp., Shedorhinotermes sp., and Capritermes sp.. The frequency of termite attacks on the test site reached 93.1%. Rubberwood was the most potential wood bait for subterranean termites, indicated by the highest average weight loss value (65.8%) with a shorter optimal baiting time (up to one month) than that of other tested woods.

• BMB Reports
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• 제44권1호
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• pp.52-57
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• 2011

Termites play an important role in the degradation of dead plant materials and have acquired endogenous and symbiotic cellulose digestion capabilities. The feruloyl esterase enzyme (FAE) gene amplified from the metagenomic DNA of Coptotermes formosanus gut was cloned in the TA cloning vector and subcloned into a pET32a expression vector. The Ft3-7 gene has 84% sequence identity with Clostridium saccharolyticum and shows amino acid sequence identity with predicted xylanase/chitin deacetylase and endo-1,4-beta-xylanase. The sequence analysis reveals that probably Ft3-7 could be a new gene and that its molecular mass was 18.5 kDa. The activity of the recombinant enzyme (Ft3-7) produced in Escherichia coli (E.coli) was 21.4 U with substrate ethyl ferulate and its specific activity was 24.6 U/mg protein. The optimum pH and temperature for enzyme activity were 7.0 and $37^{\circ}C$, respectively. The substrate utilization preferences and sequence similarity of the Ft3-7 place it in the type-D sub-class of FAE.