Abstract:
Laccase (EC 1.10.3.2, p-diphenol:dioxygen oxidoreductase) is a coppercontaining
polyphenol oxidase. The laccase enzyme can be produced by fungi.
One of the fungi is Trichoderma asperellum. T. asperellum LBKURCC1 is one
of the fungi that isolated from the cocoa plantations. The activity of the laccase
enzyme is influenced by several factors, including pH and temperature. The
purpose of this research was to determine the activity of the laccase enzyme at
various pH and temperature using a microplate reader λ 405 nm. In this research,
laccase was partially purified by the precipitation method of ammonium sulfate
20-80% and dialysis using ultrafiltration centrifugation (UF) with a membrane of
30,000 Dalton Molecular Weight Cut Of (MWCO) and the activity of the laccase
enzyme was tested using the Microplate reader method. Based on this research,
the highest activity of the laccase enzyme T. asperellum LBKURCC1 on ABTS
was found to be at optimum pH (5.5 and 4.0) and an optimum temperature of
45oC, giving a laccase activity of (65.16 ± 14.26 and 59.83 ± 5.25) and
(224.66 ± 17.39) U/L respectively.
