KARAKTERISASI LIPASE TERMOSTABIL (ISOLAT AL96) BERDASARKAN PARAMETER TEMPERATUR DAN pH PADA INDUSTRI MAKANAN
DOI:
https://doi.org/10.22373/lj.v7i1.4696Keywords:
thermostable lipase, isolate AL96, ammonium sulphate fractions, characterization of lipase, food industryAbstract
This research aims to produce large amounts of lipase and have high activity so that it can be utilized in the food industry. Method of Research used a thermostable enzyme derived from compost AL96 microorganisms. Qualitative tests are carried out using Thermus media. Extracellular lipase enzyme expressed by AL96 culture at 700C for 17 hours was isolated as much as 1000 mL and the crude extract obtained was deposited by fractionation of ammonium sulfate. After obtaining a fraction of 0-30%; 30 -50% fraction; 50-70% fraction; and 7-90% fraction was then tested for lipase enzyme activity using spectrophotometric techniques and testing of protein content determined by the Bradford method. Results Of research obtaining partial purification using ammonium sulfate into crude enzyme extract from AL96 isolate with a fraction of 50-70% resulted in the highest specific activity of protein 0.018 U / mg. Further analysis of lipase in the 30-50% fraction has the optimum temperature at 65 0C and the fraction of 50-70% has the optimum temperature at 75 0C. Characterization of the optimum pH for 50-70% fraction and 30-50% fraction showed that both fractions had optimum pH 10.References
Bradford, M., M. (1976). A Rapid and Sensitive Method for The Quantitation Microgram Quantities of Protein Utilizing The Principle of Protein-Dye Binding. Analytical Biochemistry, 72, 248 – 254.
Cutler, P. (2004). Protein Purification Protocol Second Edition Method in Molecular Biology. Human Press, 244, 24 – 26.
Fardiaz, S. (1992). Analisis Mikrobiologi Pangan. Jakarta: Raja Grafindo Persada.
Jegannathan RK, Nielsen HP. (2013). Environmental Assessment of Enzyme Use in Industrial Production. Journal of Cleaner Production. 42, 22.
Lee, D., Koh, Y., Kim, K., Choi, H., Kim, D., Suhartono, M. T., dan Pyun, Y. (1999). Isolation and Characterization of a Thermophilic Lipase from Bacillus thermoleovorans ID-1, FEMS Microbiology Letters, 179, 393 – 400.
Nurhasanah. (2015). Kloning, Karakterisasi Dan Ekpresi Gen Pengkode Lipase Termostabil dari Kompos Melalui Pendekatan Metagenom, Disertasi Program Doktor, Institut Teknologi Bandung.
Ogunbanwo S. T and Adewara, A. O. (2013). Effects of Processing Variables on The Production Of ‘Burukutu’, A Nigerian Fermented Beverage. Nature and Science Journal, 1-11.
Sari, D. K. (2010). Modifikasi Lipase Isolat Lokal pada Sintesis Biodiesel, Tesis Program Magister, Institut Teknologi Bandung.
Sambrook, J., Fritsch, E. F., Maniatis, T. (1989). Molecular cloning : a Laboratory Manual 3rd edition, USA : Cold Spring Harbor Laboratory Press, 18.47.
Scopes, R. K., (1994). Protein Purification Principles and Practice. New York: Spiringer-Verley Inc.
Sharma, S., dan Kanwar, S. S. (2014). Organic Solvent Tolerant Lipases and Applications. Scientific World Journal, 1 – 16.
Suhartono, M.T. (1989). Enzim dan Bioteknologi. Bogor: PAU Bioteknologi IPB.
Zeikus, G.J., dan Vieille, C. (2001). Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms For Thermostability, 65, 1 – 43.
Downloads
Published
Issue
Section
License
Proposed Policy for Journals That Offer Open Access Authors who publish with Lantanida Journal agree to the following terms: a. Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgment of the work's authorship and initial publication in this journal. b. Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgment of its initial publication in this journal. c. Authors are permitted and encouraged to post their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work (See The Effect of Open Access).
