PENENTUAN AKTIVITAS ENZIM LAKASE T. asperellum LBKURCC1 PADA BEBERAPA VARIASI pH dan SUHU MENGGUNAKAN MICROPLATE READER λ 405 nm

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.