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Optimasi Media Produksi, Pemurnian dan Amobilisasi Desaturase dari Absidia corymbifera (Cohn) Sacc. & trotter Untuk Meningkatkan Ketidakjenuhan Minyak Sawit Kasar

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• Code	CallNo	Lokasi	Ketersediaan
  D1038	D1038	Perpustakaan Sekolah Pascasarjana	Tersedia

• Perpustakaan	Sekolah Pascasarjana
  Judul Seri	-
  No. Panggil	D1038
  Penerbit	: Bandung., 2006
  Deskripsi Fisik	-
  Bahasa	Indonesia
  ISBN/ISSN	-
  Klasifikasi	NONE
  Tipe Isi	-
  Tipe Media	-
  Tipe Pembawa	-
  Edisi	-
  Subyek	Optimasi Media Produksi Pemurnian dan Amobilisasi Desaturase dari Absidia
  Info Detil Spesifik	-
  Pernyataan Tanggungjawab	-

• Kapang Absidia corymbifera memiliki kemampuan menghasilkan enzim desaturase. Enzim desaturase merupakan enzim intraselular yang memegang peran kunci dalam jalur sintesis asam lemak tak jenuh tunggal maupun majemuk. Kemampuan enzim desaturase ini digunakan untuk meningkatkan ketidakjenuhan asam lemak minyak sawit kasar (CPO, Crude Palm Oil). Peningkatan ketidakjenuhan asam lemak CPO membuka peluang untuk diversifikasi produk CPO. Tujuan dari penelitian ini adalah untuk mencapai produksi optimal desaturase dari kapang A. corymbifera, pemurnian dan mengetahui pengaruh aktivitas protease terhadap aktivitas desaturase serta amobilisasi enzim desaturase yang digunakan pada biokonversi untuk peningkatan ketidakjenuhan asam lemak CPO. Media sintetik Serrano-Careon et al. (1993) digunakan sebagai media fermentasi dengan rasio C/N 12,5; 19, 38. Sumber C yang digunakan adalah molases dan sukrosa, sumber N amonium sulfat dan kalium nitrat, kisaran pH 4-6, diinkubasikan pada suhu ruang selama 24, 48, 72, 96 dan 120 jam. Pertumbuhan kapang diukur berdasarkan berat kering biomassa sel. Waktu optimum produksi desaturase ditentukan berdasarkan saat aktivitas maksimum tercapai. Isolasi enzim desaturase dilakukan melalui ekstraksi buffer sitrat, presipitasi amonium sulfat dan kromatografi kolom Sephadex G-75. Hasil fraksionasi dianalisis aktivitas protease, kadar protein, elektroforesis denaturasi (SDS-PAGE, Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoreses) dan nondenaturasi protein gel poliakrilamida. Konversi CPO dilakukan dengan menambahkan fraksi enzim desaturase (1:1,b/v). Produk biokonversi CPO dianalisis bilangan iod, komposisi asam lemak dengan kromatografi gas (GC, Gas Chromatography), dan aktivitas desaturase selama penyimpanan. Proses amobilisasi desaturase dilakukan dengan teknik adsorpsi pada zeolit. Pengaturan rasio C/N dan komposisi media mampu meningkatkan produksi enzim desaturase. Komposisi media fermentasi dengan rasio C/N 19, sumber C molases dan sumber N amonium sulfat, pH 4,5 masa inkubasi selama 72 jam memberikan bobot kering biomassa tertinggi sebesar 0,87 g/250 mL serta waktu optimum produksi dan aktivitas desaturase tertinggi sebesar 2,72 U/mL. Proses pemurnian enzim dapat meningkatkan aktivitas spesifik. Nilai aktivitas spesifik enzim desaturase pada larutan ekstrak kasar sebesar 1,54 U/mg dengan kandungan protein 1,75 mg/mL. Hasil fraksionasi dengan kromatografi kolom Sephadex G-75 mempunyai aktivitas spesifik sebesar 3,98 U/mg dengan kandungan protein 0,55 mg/mL. Hasil analisis GC produk biokonversi CPO menunjukkan adanya peningkatan kandungan asam lemak oleat, linoleat dan linolenat sebesar 0,27%; 9,9% dan 96,6%. Proses amobilisasi dapat mempertahankan stabilitas enzim selama delapan jam dibandingkan tanpa amobilisasi yang bertahan selama lima jam. Fungus of Absidia corymbifera has ability to produce desaturase enzymes. Desaturase enzymes are intracellular enzymes playing key role in the synthesis of mono and polyunsaturated fatty acids. This desaturase ability was used to increase unsaturated level CPO (Crude Palm Oil). The increase of unsaturated level of CPO has opened the possibility of product diversification of CPO. The objective of this research is to reach the optimum production of desaturase enzyme from A. corymbifera, purification of desaturase, the influence of protease activity to the desaturase activity, and immobilization of desaturase enzyme for bioconversion to increase the unsaturated level of CPO fatty acids. Synthetic media of Serrano-Careon et al. (1993) was used as a fermentation media with C/N ratio 12.5; 19; 38. The C source used, was molasses and sucrose while the N source was ammonium sulphate and potassium nitrate, pH range of 4-6, incubated at room temperature for 24, 48, 72, 96, 120 hours. Growth of the fungi was measured as biomass dry weight on the fungal cells. Optimum production of desaturase was determined based on the time at maximum activity. The isolation of desaturase enzyme was carried out with citrate buffer extraction, ammonium sulphate precipitation and column chromatography Sephadex G-75. The results of every fraction, their protease activity, and concentration of protein, SDS-PAGE (Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoreses) and nondenaturation of gel polyacrylamide were analyzed. The CPO bioconversion was conducted by adding desaturase enzyme fraction (1:1, w/v). The bioconversion product of CPO was analyzed its iodine value, desaturase activity, and fatty acid composition, using gas chromatography (GC) and the desaturase stability during preservation. The desaturase immobilization was conducted by adsorption using zeolite. The arrangement of C/N ratio and media composition was capable to increase production of desaturase enzyme. The composition of fermentation medium with C/N ratio 19, molasses and ammonium sulphate as N source pH 4.5 with incubation time for 72 hours produced highest dried biomass as much as 0.87 g/250 mL and the optimum production time and highest desaturase activity as much as 2.72 U/mL. Enzyme purification process could increase specific activity. The value of specific activity desaturase of the crude extract solution was 1.54 U/mg with protein concentration as much as 1.75 mg/mL. The fraction of column chromatography Sephadex G-75 has highest specific activity as much as 3.8 U/mg and protein concentration of 0.55 mg/ mL The GC analysis result of the bioconversion product of CPO showed the increase of unsaturated fatty acid content of oleic, linoleic and linolenic acids were 0.27%; 9.9% and 96.6%, respectively. The immobilization process of the enzyme could keep enzyme stability for eight hours while non immobilized enzyme stable for five hours.

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