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BIODELIGNIFICATION OF AGRO-INDUSTRIAL WASTE AS THE SUBSTRATE TO PRODUCE LACCASE ENZYME FROM TRAMETES VERSICOLOR Perdani, Meka Saima; Malisi, Sibro; Putri, Dwini Normayulisa; Margaretha, Grace; Hermansyah, Heri
BAROMETER Vol 9 No 1 (2024): Barometer
Publisher : Fakultas Teknik, Universitas Singaperbangsa Karawang

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.35261/barometer.v9i1.11018

Abstract

Agro-industrial waste in Indonesia is a significant problem for the environment. Optimization of agro-industrial waste utilization is an exciting thing to be researched further. This study aims to utilize agro-industrial waste to optimize laccase enzyme production. The agro-industrial waste used is in the form of bagasse, rice straw, and corn stalks. The waste is used as biomass and treated to extract cellulose through bio-delignification. Cellulose serves as a substrate substance in the production of laccase enzymes. Laccase enzymes can be applied as a biocatalyst in the environmental, pharmaceutical, and chemical industries. Cellulose from agroindustry waste was synthesized by heat treatment using steam explosion with the operation conditions 200°C and 10 bar for 10 minutes. The production of laccase enzymes was done using the green technology submerged fermentation method for 32 hours at 25°C. The optimal result in producing laccase enzyme is using substrate from corn stalks and adding nutrients with an activity value of 25.46 U/mL. The reaction kinetics of laccase enzyme and commercial enzyme against 0.1 M substrate were modelled using the Euler method, and the k value was 2x10-4 min-1 (crude laccase) and 1.9x10-2 min-1 (commercial laccase).
Determination of the Kinetic Parameters of Cholesterol Oxidation using Cholesterol Oxidase from Streptomyces sp. Perdani, Meka Saima; Hermansyah, Heri; Sahlan, Muhamad; Putri, Dwini Normayulisa; Pambudi, Teguh; Hasibuan, Anggi Khairina Hanum
Makara Journal of Technology Vol. 28, No. 3
Publisher : UI Scholars Hub

Show Abstract | Download Original | Original Source | Check in Google Scholar

Abstract

Cholesterol oxidase (CO) was successfully produced from Streptomyces sp. via the submerged fermentation method, and 69 U/mL enzyme activity was obtained. This study aimed to determine cholesterol oxidation kinetics and the production of CO as a catalyst. The enzyme was diluted to 0.15, 0.075, and 0.00375 U/mL for the oxidation reaction. The substrate was also prepared in three concentrations: 3.23, 6.46, and 12.93 mM. The optimization of conditions for enzymatic cholesterol oxidation was investigated through measurement of the effect of initial cholesterol and enzyme concentrations. Cholesterol concentration was rapidly measured via high-performance liquid chromatography (HPLC). The kinetics of CO were modeled using the first-order irreversible reaction. An enzymatic kinetic model was derived, and it was verified using experimental data and sensitivity analysis. Based on the experiment, the highest enzyme concentrations of crude and commercial CO can oxidize the substrate up to 84% within 240 min. However, the oxidation reaction showed a slightly different behavior in the early 60 min, and crude CO exhibited a slower substrate oxidation. The kinetic rate constant obtained by Euler’s method reached 1.0 x 10−3/min and 1.41 x 10−3/min for 0.15 U/mL crude and commercial CO, respectively.