ISSN: 0973-7510

E-ISSN: 2581-690X

Research Article | Open Access
Deviyanthi Nur Afifah1,2, Suharti3, Syifa F. Syihab1,4 and Akhmaloka1,3
1Biochemistry Research Group, Faculty of Mathematics and Natural Science, Institut Teknologi Bandung, Indonesia, Jl. Ganesha 10, Bandung – 40132 Indonesia.
2Study Program of Pharmacy, Institut Kesehatan Indonesia, Indonesia, Jl. Boulevard Barat Raya, North Jakarta – 14240 Indonesia.
3Department of Chemistry, Faculty of Science and Computer, Universitas Pertamina, Indonesia, Jl. Teuku Nyak Arief, South Jakarta – 12220 Indonesia.
4Faculty of Sports and Health Education, Universitas Pendidikan Indonesia, Indonesia, Jl. DR. Setiabudi No.229, Bandung – 40154 Indonesia.
J. Pure Appl. Microbiol., 2019, 13 (4): 2195-2199 | Article Number: 5789
https://doi.org/10.22207/JPAM.13.4.32 | © The Author(s). 2019
Received: 16/08/2019 | Accepted: 06/11/2019 | Published: 11/12/2019
Abstract

Lipase (Triacylglycerol acyl hydrolase), is a hydrolase enzyme that plays an important role in industries such as health, food, biotechnology, and energy. Lipase might be isolated from almost all living organism, either higher organisms or microbes. In this report, lipase was isolated from compost isolated microbe namely AL89 isolate. AL89 was previously identified closed to Pseudoxanthomonas taiwanensis. The crude extract of lipase was produced by incubating of the culture at 55°C for 19 hours. The crude extract was partially purified using acetone fractionation. Fractionation was carried out at concentrations of acetone at 0-20%, 20-40% and 40-60%. The specific activity was determined by hydrolytic activity of lipase with the substrate of para-nitrophenylpalmitate (pNPP). The result showed that the highest activity of the enzyme is 0.0971 U/mg protein from the fraction of 0-20%. Lipase from isolate AL89 showed optimum activity at 55°C and pH 9. In addition the enzyme prefers para-nitrophenyl laurate (pNPL) as substrate. Using zymography analysis showed that the active protein at the size of 70 kDa. All the data suggested the enzyme is thermo and alkali-tolerant lipase.

Keywords

Biotechnology, lipase enzyme, isolate AL89, microorganisms, compost.

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