Abstract:
Trichoderma asperellum LBKURCC1 is one of the biocontrol agents capable of
producing the enzyme laccase. Laccase (EC 1.10.3.2) is an extracellular enzyme that
contains copper ions and catalyzes the four-electron oxidation of various -OH containing
substrates. T. asperellum LBKURCC1 laccase is able to oxidize several triphenylmethane
textile dyes, including Bromocresol purple (BCP) dye. This study explores chemical
changes of the dye, Bromocresol purple (BCP) by treatment with crude extracts of T.
asperellum LBKURCC1 by analyzing its Fourier Transform Infra Red (FTIR) spectrum
to determine changes in functional groups. The FTIR results did not show any addition
or reduction of functional groups in BCP buffer controls, in BCP treated with the inactive
enzyme, and with BCP treated with the active enzyme for 30 minutes and 6 days,
respectively. However, there was a slight difference in the FTIR spectrum between 30
minutes and 6 days treatments, for all experiments, namely a decrease in the stretching of
2850 cm-1 due to the widening of the O-H stretching. This indicates that BCP is oxidized
and leads to a more polar compound because the intensity of the O-H stretch increases
and C-H which is a non-polar group decreases.
