Isolation of Lipase from Candlenut Seeds and Its Immobilization in Polyacrylamide Gel
DOI:
10.29303/jppipa.v8i3.1483Published:
2022-07-31Issue:
Vol. 8 No. 3 (2022): JulyKeywords:
lipase, Candlenut, Activity, Immobilization, PolyacrylamideResearch Articles
Downloads
How to Cite
Downloads
Metrics
Abstract
In general, lipase enzymes are used in the form of free lipase enzymes which can only be used once and are less effective, so that their use is costly. Therefore, to maximize the use of the lipase enzyme, immobilization of the enzyme that allows multiple use is a choice. The purpose of this study was to determine the activity of the candlenut (Aleurites moluccana (L.) Wild) lipase in its free form and in immobilization form. The stability of the immobilized lipase enzyme with repeated use was also investigated. The enzyme was immobilized by trapping method using polyacrylamide gel. The immobilized lipase enzyme was characterized to determine its stability after repeated use with various gel concentrations. The crude extract of the lipase of candlenut seed sprouts had an activity of 2.32 U/mL, whereas the activity of the immobilized lipase enzyme in polyacrylamide gel at concentrations of 6%, 8%, and 10%, were 2.133; 2,259; and 2,311 U/mL, respectively. The optimum temperature for the immobilized lipase enzyme was 30 oC and the optimum pH was 7.5. After five time us usage, the immobilized enzyme showed activities of 49.49%, 72.60% and 86.53%, for 6%, 8% and 10% polyacrylamide gel, respectively. These results indicate that the immobilized lipase enzyme from seed sprouts of candlenut (Aleurites moluccana (L.) Wild) by trapping method using 10% polyacrylamide gel can maintain its stability after five times of useReferences
Bilal, M., Asgher, M., Cheng, H., Yan, Y., & Iqbal, H. M. N. (2019). Multi-point enzyme immobilization, surface chemistry, and novel platforms: a paradigm shift in biocatalyst design. Critical Reviews in Biotechnology, 39(2), 202–219. https://doi.org/10.1080/07388551.2018.1531822
Djarkasi, G. S. S., Raharjo, S., & Noor, Z. (2017). Isolation and Specific Activity of Indigenous Lipase Enzyme in Canarium Nut. Jurnal Teknologi Pertanian, 8, 28–35. DOI: https://doi.org/10.35791/jteta.8.1.2017.16349
Dzulkarnain, D. (2018). Isolation and determination of optmum lipase works condition from durian seed germination (Durio zibethinus L). Prosiding Seminar Nasional Kimia 2018, 31–33. Retrived from http://jurnal.kimia.fmipa.unmul.ac.id/index.php/prosiding/article/download/751/478/
Enujiugha, V. N., Thani, F. A., Sanni, T. M., & Abigor, R. D. (2004). Lipase activity in dormant seeds of the African oil bean (Pentaclethra macrophylla Benth). Food Chemistry, 88(3), 405–410. https://doi.org/10.1016/j.foodchem.2004.01.052
Firdaus, F., Dali, S., & Rusman, H. J. (2017). Imobilisasi Enzim Lipase Dedak Padi (Oryza sativa L) pada Karbon Aktif: Karakterisasi dan Uji Stabilitas Kerja Enzim Imobil. Indonesia Journal of Chemistry Research, 5(1), 32–36. DOI: https://doi.org/10.30598//ijcr.2017.5-fir
Kawiński, A., Miklaszewska, M., Stelter, S., Głąb, B., & Banaś, A. (2021). Lipases of germinating jojoba seeds efficiently hydrolyze triacylglycerols and wax esters and display wax ester-synthesizing activity. BMC Plant Biology, 21(1), 1–14. https://doi.org/10.1186/s12870-020-02823-4
Kumar, R. R., Bhargava, D. V., Pandit, K., Goswami, S., Mukesh Shankar, S., Singh, S. P., Rai, G. K., Tara Satyavathi, C., & Praveen, S. (2021). Lipase – The fascinating dynamics of enzyme in seed storage and germination – A real challenge to pearl millet. Food Chemistry, 361, 130031. https://doi.org/10.1016/j.foodchem.2021.130031
Kumar, S., Yadav, R. K., & Negi, S. (2014). A comparative study of immobilized lipase produced from Penicillium chrysogenum SNP5 on two different anionic carriers for its pH and thermostability. Indian Journal of Biotechnology, 13(3), 301–305. Retrieved from http://nopr.niscpr.res.in/bitstream/123456789/29607/1/IJBT%2013%283%29%20301-305.pdf
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature, 227, 680–685. DOI: 10.1038/227680a0
Minovska, V., Winkelhausen, E., & Kuzmanova, S. (2005). Lipase immobilized by different techniques on various support materials applied in oil hydrolysis. Journal of the Serbian Chemical Society, 70(4), 609–624. https://doi.org/10.2298/JSC0504609M
Monnet, T. Y., Kouadio, P., Koffi, B., Soro, Y. R., & Dué, E. A. (2012). Biochemical characterization of the lipase activities in dormant seeds from the ripe and unripe Terminalia catappa Linn ( Myrtales : Combretaceae ) fruits harvested in Côte d ’ Ivoire. Journal of Applied Biosciences, 49, 3371–3382. Retrieved from https://www.m.elewa.org/Journals/jabs-volume-49-january-2012/
Mubarik, N. R. (2001). Imobilisasi protase bacillus subtilis ATCC 6633 menggunakan MAtriks Gel Poliakrilamida. Hayati, 8(1), 11–14. Retrieved from https://www.google.com/url?sa=t&rct=j&q=&esrc=s&source...mfh1riSU4
Mulko, L., Pereyra, J. Y., Rivarola, C. R., Barbero, C. A., & Acevedo, D. F. (2019). Improving the retention and reusability of Alpha-amylase by immobilization in nanoporous polyacrylamide-graphene oxide nanocomposites. International Journal of Biological Macromolecules, 122, 1253–1262. https://doi.org/10.1038/s41598-022-07229-w
Permana, I. D. M., Indrati, R., Hastuti, P., & Suparmo. (2013). Indogenous Lipase Activities during Cocoa Bean ( Theobroma cacao L .) Germination. Agritech, 33(2), 176–181. https://doi.org/10.22146/agritech.9795
Sattar, H., Aman, A., Javed, U., & Ul Qader, S. A. (2018). Polyacrylamide beads: Polymer entrapment increases the catalytic efficiency and thermal stability of protease. Molecular Catalysis, 446, 81–87. https://doi.org/10.1016/j.mcat.2017.12.022
Savalas, L. R. T., Sirodjudin, S., Gunawan, E. R., Aini, R., Suhendra, D., Basri, N. H., ’ardhuha, J., & Ningsih, B. N. S. (2021). Biochemical properties of coconut (Cocos nucifera l.) lipase. Philippine Journal of Science, 150(5), 915–924. Retrived from https://philjournalsci.dost.gov.ph/publication/regular-issues...nucifera-l-lipase
Sya’bani, N., Astuti, W., & Pratiwi, D. R. (2017). Isolasi dan karakterisasi lipase dari kecambah biji alpukat (Persea americana Mill) Isolation and characterization of lipase from germinated avocado (Persea americana Mill) seeds. Jurnal Atomik, 02(2), 209–212. Retrieved from http://jurnal.kimia.fmipa.unmul.ac.id/index.php/JA/article/view/486
Tambun, R., Tambun, J. O. A., Tarigan, I. A. A., & Sidabutar, D. H. (2020). Activating Lipase Enzyme in the Candlenut Seed to Produce Fatty Acid Directly from Candlenut Seed. Journal of Physics: Conference Series, 1542(1). https://doi.org/10.1088/1742-6596/1542/1/012006
Taurina, W., & Andrie, M. (2021). The Determination of Total Protein Levels in the Water Phase of Snakehead Fish Extract (Channa Striata) Before and After Freeze Dry using the Biuret Method. Journal of Pharmaceutical Sciences and Research, 13(10), 630–634. Retrieved from https://www.proquest.com/docview/2595666488?pq-origsite=gscholar&fromopenview=true
Tavares, F., Petry, J., Sackser, P. R., Borba, C. E., & Silva, E. A. (2018). Use of castor bean seeds as lipase source for hydrolysis of crambe oil. Industrial Crops and Products, 124(June), 254–264. https://doi.org/10.1016/j.indcrop.2018.06.073
Thangaraj, B., & Solomon, P. R. (2019). Immobilization of Lipases – A Review. Part II: Carrier Materials. ChemBioEng Reviews, 6(5), 167–194. https://doi.org/10.1002/cben.201900017
Wardoyo, F. A., Raharjo, T. J., Swasono, R. T., Semarang, U. M., & Mada, U. G. (2015). Uji Stabilitas Enzim Lipase Terimobilisasi Pada Kitosan. University Research Coloquium, 2, 254–259. Retrieved from https://jurnal.unimus.ac.id/index.php/psn12012010/article/view/1596
Zhao, X., Qi, F., Yuan, C., Du, W., & Liu, D. (2015). Lipase-catalyzed process for biodiesel production: Enzyme immobilization, process simulation and optimization. Renewable and Sustainable Energy Reviews, 44, 182–197. https://doi.org/10.1016/j.rser.2014.12.021
Zou, B., Yan, Y., Xia, J., Zhang, L., & Adesanya, I. O. (2020). Enhancing bio-catalytic activity and stability of lipase nanogel by functional ionic liquids modification. Colloids and Surfaces B: Biointerfaces, 195(301). https://doi.org/10.1016/j.colsurfb.2020.111275
Author Biographies
Zella Yaumin Nasry, University of Mataram
Nyoman Maya Krisnawati, University of Mataram
Erin Ryantin Gunawan, University of Mataram
Jannatin ‘Ardhuha, University of Mataram
Agus Abhi Purwoko, University of Mataram
Lalu Rudyat Telly Savalas, University of Mataram
License
Copyright (c) 2022 Zella Yaumin Nasry, Nyoman Maya Krisnawati, Erin Ryantin Gunawan, Jannatin ‘Ardhuha, Agus Abhi Purwoko, Lalu Rudyat Telly Savalas
This work is licensed under a Creative Commons Attribution 4.0 International License.
Authors who publish with Jurnal Penelitian Pendidikan IPA, agree to the following terms:
- Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution 4.0 International License (CC-BY License). This license allows authors to use all articles, data sets, graphics, and appendices in data mining applications, search engines, web sites, blogs, and other platforms by providing an appropriate reference. The journal allows the author(s) to hold the copyright without restrictions and will retain publishing rights without restrictions.
- 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 Jurnal Penelitian Pendidikan IPA.
- 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).