Ludwinardo Putra, Irma Kresnawaty, Imron Riyadi

Characterisation of novel acidic lipase of Corynebacterium nuruki PM2 from palm oil mill effluent for palm oil derivatisation

Introduction

Characterisation of novel acidic lipase of corynebacterium nuruki pm2 from palm oil mill effluent for palm oil derivatisation. Discover a novel acidic lipase from Corynebacterium nuruki PM2 isolated from palm oil mill effluent. Characterized for palm oil derivatization, it shows optimum activity at 40-60°C & pH 5-8, stable in solvents.

Abstract

The palm oil industry generates significant amounts of palm oil mill effluent (POME), which harbors diverse microbial communities with potential biotechnological applications. Yet, only a limited number of lipolytic bacteria have been isolated and studied. A limited nutrient medium selection has been previously demonstrated for isolating unique indigenous bacteria. This study aimed to isolate novel lipolytic bacteria from POME and characterize the lipase for potential palm oil derivatization. Corynebacterium nuruki PM2 was successfully isolated and identified. Distinct colony morphologies were observed on different agar media. Lipase from C. nuruki PM2 (LipCN) exhibited optimum activity at 40-60°C, pH 5.0-8.0, and with vegetable oil as substrate. The enzyme also showed the highest stability at a temperature between 30 °C and 40°C and at a pH of 7.0-8.0 after 30 minutes of incubation. The enzyme remained stable in methanol, isopropanol, and n-hexane. Metal ions such as Mn2+ and surfactants (e.g., Triton X-100, Tween-80, and Tween-20 significantly inhibit LipCN activity. Thin-layer chromatography identified 2-palmitoylglycerol in the hydrolyzed product of LipCN, suggesting sn-1,3 specific activity of the enzyme.

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