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"Ruang Lingkup dan Cara Penelitian:Karies merupakan penyakit yang paling banyak ditemukan dalam rongga mulut Proses karies diawali dengan pembentukan plak pada permukaan gigi. Plak merupakan lapisan yang mengandung sel-sel kuman dan bahan-bahan organik yang melekat pada gigi. S. mutans serotipe c merupakan kuman asidogenik yang paling dominan dalam plak dan tahan terhadap lingkungan asam. Kuman ini mensintesis polisakarida (glukan) ekstraseluler yang tidak larut dalam air dan bersifat lengket sehingga dapat membentuk agregrat antar kuman. Pembentukan glukan dikatalisis oleh enzim glukosiltransferase (GTF) yang menggunakan sukrosa sebagai substrat. Selanjutnya kuman-kuman dalam plak menghasilkan asam dari metabolisme karbohidrat makanan yang menyebabkan terjadinya demineralisasi jaringan keras gigi. GTF diisolasi dari S. mutans serotipe c INA99 untuk menghambat terjadinya karies gigi pada tikus coba. Namun sifat-sifat biokimia GTF dari kuman ini belum diketahui. Penelitian ini bertujuan untuk mengisolasi dan mempelajari sifat-sifat GTF dari S. mutans serotipe c 1NA99. GTF diisolasi dari biakan cair S. mutans dalam Brain Heart Infusion Yeast (BHIY). Tahap isolasi selanjutnya menggunakan teknik salting out dan kromatografi afinitas sefarosadekstran T10. Karakterisasi dilakukan dengan menguji aktivitas GTF pada berbagai pH lingkungan, suhu inkubasi, waktu dan suhu penyimpanan.Hasil dan Kesimpulan:Pemisahan GTF dari protein lain dengan teknik kromatografi afinitas menghasilkan 1 puncak. Pada pengujian aktivitas GTF diketahui bahwa pH 7 merupakan pH inkubasi optimum dan suhu 37°C merupakan suhu inkubasi optimum. Pengujian aktivitas GTF setelah penyimpanan selama 3 minggu pada suhu -20°C memperlihatkan aktivitas paling tinggi dibandingkan penyimpanan pada suhu 0-4°C dan 25°C. Dari elektroforesis SDSPAGE 10% diperkirakan berat molekul GTF yang berasal dari kuman S. mutans serotipe c INA 99 adalah 98,71kD."

"Acetonitrile is an organic, derivative of carboxylic acid, and toxic compound. This compound has been widely used in pharmaceutical and chemical industries. Nowadays, there are more interests in acetonitrile-degrading microbes for their potential in chemical syntheses and biological detoxification of nitrile-containing wastes.The aim of this study were to isolate, select, and characterise the isolate from industrial effluents which has the best degrading capability and its acetonitrile-degrading enzyme. Cultures were grown on mineral medium with microelements and acetonitrile was added as sole source of energy, carbon, and nitrogen. Analysis to characterise the acetonitrile-degrading enzyme had been conducted with whole cells of the selected isolate. Decreasing of acetonitrile concentration and formation of its degrading products were determined by gas chromatography and ammonia analysis was done by Nessler's method.Isolate D5, identified as Corynebacterium sp., was able to grow on high concentration acetonitrile (up to 5 % v/v) and exhibited the highest specific growth rate (p) among 29 isolates which could grow on acetonitrile. When Corynebacterium D5 grew on 2 % (vlv) acetonitrile, the doubling time was 6 hours 40 minutes, the specific growth rate (p.) was 0.1 h-1, and the acetonitrile decreasing rate was 3.99 mM/h. Increasing of acetonitrile concentration would extend the doubling time, decline the maximum growth and specific growth rate (M), and biomass production. The products of acetonitrile degradation by Corynebacterium D5 were acetamide, acetic acid, and ammonia. The highest maximum growth of Corynebacterium D5 showed when 13-aminopropionitrile was used as a substrate.Corynebacterium D5 degraded 5 % (v/v) acetonitrile with degrading rate of 0.906 µmol min-' (mg dry weight cells)-'. Corynebacterium D5 hydrolysed acetonitrile by two-step reaction catalysed by nitrile hydratase and amidase. The acetamide forming rate [0.399 pmol min' (mg dry weight cells)-' ] was higher than acetic acid forming rate [0.198 µcool min-' (mg dry weight cells)'' ] and the maximum acetamide concentration formed (about 239 mM) was also higher than maximum acetic acid concentration formed (about 145 mM). Nitrite hydratase activity of Corynebacterium D5 was found to be higher than amidase activity. Maximum nitrite hydratase activity was found out at pH 6 and at 30 °C, while maximum amidase activity was found out at pH 7 and up to 60 °C the activity still increase. Nitrite hydratase of Corynebacterium D5 was totally inhibited by 5 mM Hg2+, whereas amidase was slightly inhibited by 10 mM Co2+."

"Fosfatase asam merupakan enzim yang dapat digunakan untuk teknik ELISA - untuk mengukur kadar suatu zat dalam cairan tubuh yang jumlahnya sangat kecil. Salah satu sumber enzim tersebut adalah air kelapa (Cocos nucifera Linn). Penelitian yang dilakukan oleh Sadavisan (1951), Wilson et al. (1952), Anna Istiqomah (1994) dan Emilia Aisjah (1996) menunjukkan adanya aktivitas enzim fosfatase dalam daging buah dan air kelapa.Penelitian ini adalah mengisolasi dan pemurnian enzim fosfatase asam dari air kelapa. Untuk pemurnian enzim digunakan kromatografi gel dengan Sephadex G-75 dan kromatografi afinitas dengan Gel immobilized p-aminobenzyl phosphonic acid sepharose. Kemurnian enzim diperiksa dengan elektroforesis gel poliakrilamid. Aktivitas enzim secara kuantitatif ditentukan dengan spektrofotometer, dan secara kualitatif dapat dilihat dengan pewarnaan substrat. Kadar protein diukur dengan spektrofotometer pada panjang gelombang 280 nm.Hasil.penelitian ini menunjukkan bahwa dalam air kelapa terdapat enzim fosfatase asam yang ditunjukan oleh satu pita pada elektroforesis gel poliakrilamid.

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Isolation And Purification Of Acid Phosphatase From Coconut Water (Cocos nucifera Linn)Acid phosphatase was detected in coconut. More than fourty years ago, early investigators found this enzyme solely in coconut milk. It is not until recently that the enzyme was also found in coconut water. Recent studies also reported some characteristics of the enzyme from both sources.The purpose of this study is to isolate and to purity acid phosphatase from coconut water. Firstly, the enzyme was precipitated with etanol. After the dialysis in a cellophane bag, the precipitate was redissolved in 0,9% NaCl. The enzyme was separated with Sephadex 0-75, using 0,9% NaCl as eluent. Fractions of 5 mL were collected and each was analysed for the protein contents and for acid phosphatase activities. The fractions of high enzymes activity were pooled and purified, using an affinity chromatography technique with benzoyl phosphonic acid, a competitive inhibition, as a stationary immobilized ligand. Retained enzymes were eluted with 0,2 M NaHHPO4 and fractions of 2 mL were collected.During the study, protein contents were measured with A 280 technique and enzymes activities were assayed with p-nitrophenyl phosphate (p-NPP) as a substrate. In both steps, the purity of the pooled fractions were analysed with a polyacrylamide gel electrophoresis, stained with Coomassie Blue as well as p-NPP-ammonium sulfide, lead acetat for revealing the enzyme.It is found that acid phosphatase could be isolated and purified, as indicated by increasing specific activity and by PAGE analysis, from coconut water, by gel filtration and affinity chromatography technique."

"Ruang Lingkup dan Cara Penelitian: Enzim fosfatase alkali antara lain digunakan dalam teknik ?enzyme immunoassay?, untuk mengukur kadar sesuatu zat dalam cairan tubuh dalam jumlah yang sangat kecil. Dalam penelitian ini diusahakan isolasi dan pemurnian enzim fosfatase alkali dari E. coli. Identifikasi kuman dilakukan dengan agar Endo, agar darah, tes pewarnaan Gram, sifat-sifat biokimia, dan tes serologik. Untuk pemurnian enzim digunakan sonikator, kromatografi pertukaran ion dengan DEAE Biogel, dan kromatografi gel dengan Sephadex G-100. Kemurnian enzim diperiksa dengan elektroforesis pada membran selulosa asetat. Aktivitas enzim secara kuantitatif ditentukan dengan spektrofotometer, dan secara kuaLitatif dapat dilihat dengan agar substrat. Kadar protein diukur dengan metoda Lowry. Terhadap fraksi gel diteliti pengaruh suhu, pH, ion logam, dan jenis bufer atas aktivitas enzim. Demikian pula ditentukan nilai Km dan Vmax, serta reaksi hidrolisis tanpa dan dengan transfosforilasi.Hasil dan Kesimpulan: Kuman diidentifikasi sebagai E. coli non-patogen. Enzim diperoleh setelah fraksi gel dengan ,pemurnian 242 kali dan hasil 59%. Pada eLektroforesis ditemukan kadar protein enzim 52,8%. Enzim memiliki pH optimum 8,0, dan tidak stabil bila diinkubasi selama 1 jam diluar pH optimum. Aktivitas enzimeningkat secara Linier sampai suhu 45° C, dengan koefisien suhu 1,49. Enzim stabil pada inkubasi selama 20 menit pada suhu 25 - 45° C. Aktivitas enzim tidak dipengaruhi penambahan ion Mg dan Zn (0,01 M). Aktivitas meningkat dengan meningkatnya molaritas bufer, Vmax terbesar didapatkan dalam buffer Tris dan Km terkeciL pada bufer AMP. Reaksi hidrolisis dan transfosforilasi berlangsung pada bufer Tris dan AMP, sedangkan pada bufer glisin hanya terjadi reaksi hidrolisis.

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Scope and Method of Study: The enzyme alkaline phosphatase is used among others in enzyme immunoassay, to enable the quantitation of a small amount of substances in body fluids. In this study, an attempt was carried out for the isolation and purification of the enzyme from E. coli. The bacteria was identified through culture on Endo and blood agar, Gram staining, biochemical tests, and serology. The bacteria were disrupted by ultrasonication, and the enzyme purified by ion exchange chromatography on DEAE Biogel followed by gel chromatography on Sephadex G-100. Enzyme purity was examined by electrophoresis on cellulose acetate. Enzyme activity was determined by spectrophotometry, and protein concentration was measured by the method of Lowry. The gel fraction was tested for the effect of pH, temperature, metal ion, and type of buffer. The Km and Vmax was measured, for hydrolysis with and without transphosphorylation.Findings and Conclusions: The bacteria was identified as non-pathogenic E. coli. After gel chromatography the enzyme was purified 242 fold, at 59%, yield. Electrophoresis revealed that the enzyme content was 52.8 %. The enzyme has a pH optimum of 8.0, and it was unstable on standing for 1 hour outside the pH optimum. Enzyme activity increased Linearly with temperature (to 45° C), with a temperature coefficient of 1.49. The enzyme is stable for 20 minutes at 5° - 45++ C, and the activity not influenced by Mg++ and Zn++ ions (0.01 M). The activity increased with increased molarity of the buffer, the highest Vmax was observed with Tris buffer, and the Lowest Km with AMP buffer. Hydrolysis and transphosphorylation occurred in Tris and AMP buffer, while in glycine buffer only hydrolysis was observed."

"Tanaman Phyllanthus niruri L. (famili : Phyllantaceae) secara tradisional telah digunakan sebagai bahan obat termasuk diantaranya sebagai obat antidiabetes dan antihipertensi. Ekstrak metanol dan air dari tanaman ini telah diuji in vivo dan berpotensi sebagai antihiperglikemia dan antihipertensi.Penelitian ini bertujuan untuk mengisolasi senyawa aktif penghambat α-glukosidase dan angiotensin converting enzyme (ACE) dari ekstrak metanol P. niruri L. Simplisia kering dihaluskan dan diekstraksi dengan metanol 80%, kemudian difraksinasi dengan heksan, etil asetat, butanol dan air. Fraksi heksan dan etil asetat diisolasi menggunakan metode kromatografi kolom dengan fase diam silika gel 60 dan fraksi butanol menggunakan fase diam Sephadex LH-20. Penentuan struktur senyawa dilakukan dengan menganalisis data spektroskopi IR, MS,NMR dan membandingkan dengan pustaka.Hasil identifikasi diperoleh empat senyawa yaitu hipofillantin (1), fillantin (2), metil galat (3) dan kuersetin 3-O-β-Dglukopiranosil?(1´ ´ ´ - 6´ ´ )-α-rhamnosida (4). Pengujian efek penghambatan terhadap aktivitas enzim α-glukosidase secara in vitro menunjukkan bahwa senyawa 1-4 aktif dengan nilai IC50 masing-masing 0,14; 0,11; 0,081dan 0,023 mM. Senyawa tersebut juga menunjukkan efek penghambatan terhadap ACE dengan IC50 masing-masing 0,18; 0,14; 0,015 dan 0,086 mM.

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Phyllanthus niruri L. (family: Phyllanthaceae) is a small herb well known its medicinal properties and widely used worldwide. The methanol and aquoeous extract were studied in vivo its potential anti-hyperglicemic and anti-hypertension.The aim of present study was to isolate the α-glucosidase and angiotensin converting enzyme (ACE) inhibitor from methanol extract. Dried of its was extracted with 80% methanol and then partitioned by hexane, ethyl acetate, butanol and water. The hexane and ethyl acetate fractions were then subjected to separation and purification using silica gel chromatography and the butanol fraction using Sephadex LH-20 chromatography. The structures were determinated based on spectral analysis of IR, MS, 1D and 2D NMR and by comparison with the literature data.Four compounds were identified to be hipophyllanthine (1), phyllanthine (2), methyl gallate and quercetin 3-O-β-Dglucopyranosyl?(1´ ´ ´ - 6´ ´ )-α-rhamnoside (4). The IC50 values of α? glucosidase activity for compounds 1-4 were 0.14; 0.11; 0.081and 0.023 mM respectively. The same compounds exhibited inhibitory activity against ACE with IC50 values 0.18; 0.14; 0.015 and 0.086 mM respectively."

"Terdapat banyak metode untuk mendeteksi kontaminasi melamin dalam makanan atau produk pakan termasuk immunoassay. Dalam penelitian ini, hapten melamin disintesis dengan mereaksikan 2-kloro-4,6-diamino-1,3,5-triazina (CAAT) dengan asam 6-aminokaproat. Karakterisasi hapten dengan spektrometer Fourier Transform Infrared (FTIR) menunjukkan absorpsi ikatan N-H dari gugus amina sekunder alifatik pada frekuensi 3350-3310 cm-1 dan vibrasi ulur ikatan C-N pada daerah sidik jari 1250-1020 cm-1. Karakterisasi dengan 1H-NMR menunjukkan pergeseran kimia pada 4,20 ppm (t, 1H), sedangkan dengan 13C-NMR pada pergeseran kimia 139 ppm. Karakterisasi dengan spektrometer massa menunjukkan M+. m/z 240,4 untuk hapten (C9H16N6O2). Imunogen disintesis dengan cara menkonjugasikan hapten dengan bovine serum albumin (BSA) dengan menggunakan metode ester aktif. Konjugat hapten-BSA menyerap panjang gelombang maksimum UV pada 224 nm. Data menunjukkan bahwa hapten dan imunogen berhasil disintesis. Hapten-BSA kemudian disuntikkan ke kelinci untuk menghasilkan antibodi poliklonal. Setelah tiga minggu imunisasi, serum menunjukkan adanya antibodi melalui Gel Agarose Precipitation Test (AGPT). Dari hasil optimasi awal indirect ELISA diketahui konsentrasi optimum coating antigen hapten-OVA adalah 1 μg/mL dan konjugat HRP-anti rabbit IgG adalah 1:10.000. Dari hasil indirect competitive ELISA diperoleh bahwa pengenceran optimum antibodi yang masih memberikan respon positif berupa absorbansi yang tinggi adalah 1:125 (6 μg/mL). Antiserum yang dihasilkan memiliki sensitivitas yang cukup baik terhadap melamin dengan nilai IC50 sebesar 2,83 ppm dan limit deteksi (IC15) sebesar 0,22 ppm melalui indirect competitive ELISA.

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There are many method to detect the melamine contamination in food or feed product including immunoassay. In this study, hapten of melamine was synthesized by reacting 2-chloro-4,6-diamino-1,3,5-triazine (CAAT) and 6-aminocaproic acid. Characterization of hapten with fourier transform infrared spectroscopy (FTIR) showed secondary N-H stretching vibrational band at 3350-3310 cm-1 and C-N stretching vibrational band at fingerprint region 1250-1020 cm-1. Characterization of hapten with 1H-NMR showed chemical shift at 4,20 ppm (t, 1H), and 139 ppm by 13C-NMR. Hapten also characterized with high-resolution mass spectrometry (HRMS) that showed M+. m/z 240,4 for hapten (C9H16N6O2). The Immunogen was prepared by coupling hapten to bovine serum albumin (BSA) using the active ester method. Hapten-BSA conjugate showed the maximum wavelength of UV absorpstion at 224 nm. The data pointed out that hapten and immunogen was successfully synthesized. Hapten-BSA conjugate then injected into rabbit to produce the polyclonal antibodies. After three weeks immunization, serum showed the presence of antibodies through Agar Gel Precipitation Test (AGPT). The initial optimization of indirect ELISA showed that the optimum concentration of coating antigen hapten-OVA was 1 mg/mL and HRP-conjugated anti-rabbit IgG was 1:10,000. The optimum antibody dilution that still gave a positive response was 1:125 (6 mg/mL) through indirect competitive ELISA. Antiserum produced has a good sensitivity to melamine with IC50 2.83 ppm and a detection limit (IC15) 0.22 ppm using indirect competitive ELISA."

"Telah dilakukan penelitian mengenai variasi genetik Megalocytivirus pada kerapu tikus [Cromileptes altivelis, Valenciennes (1828)] sebagai salah satu metoda identifikasi selama bulan November 2013 - Oktober 2014. Penelitian bertujuan untuk mendeteksi keberadaan Megalocytivirus pada kerapu tikus (Cromileptes altivelis), menganalisis variasi genetik Megalocityvirus dan memperoleh metode identifikasi Megalocytivirus dengan menggunakan sekuens. Sebanyak 180 ekor ikan kerapu tikus (C.altivelis) yang diduga terinfeksi Megalocytivirus dikoleksi dari enam propinsi di Indonesia; Medan (Sumatera utara), Lampung, Batam (Kepulauan Riau), DKI Jakarta, Jepara ( Jawa Tengah) dan Bali. Jaringan limpa ikan kerapu tikus (C. altivelis) digunakan untuk pemeriksaan PCR, dan dilanjutkan sekuensing DNA. Hasil penelitian menunjukkan bahwa ikan kerapu tikus (C. altivelis) yang berasal dari enam lokasi budidaya laut terinfeksi Megalocytivirus genotype I yaitu infectious spleen and kidney necrosis virus (ISKNV). Restriction enzyme HaeII, HapII dan Ndell dapat digunakan untuk identifikasi Megalocytivirus, genotipe 1.

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Humpback Grouper (Cromileptes altivelis) were collected during the month of November 2013 - October 2014. A total of 180 Humpback Grouper (C.altivelis) are suspected of being infected Megalocytivirus collected from six locations of marine aquaculture in Indonesia; Medan (North Sumatra), Lampung, Batam (Riau Islands), Jakarta, Jepara (Central Java) and Bali. Spleen tissue of Humpback Grouper (C. altivelis) used for PCR, and DNA sequencing. The results showed that the Humpback Grouper (C. altivelis) derived from multiple locations of marine aquaculture in Indonesia haven been infected by Megalocytivirus, infectious spleen and kidney necrosis virus (ISKNV) genotype I. Restriction enzyme; HaeII, HapII and Ndell can be used for identification Megalocytivirus, ISKNV genotype 1."

"ABSTRAKGelatin merupakan salah satu jenis protein yang diperoleh dari kolagen alami yang terdapat dalam kulit dan tulang hewan. Gelatin yang paling banyak digunakan ialah gelatin babi. Penggunaan gelatin dengan bahan baku hewan babi pada produk makanan dan farmasi seringkali menyebabkan alergi, selain juga tidak diperbolehkan dalam agama islam, sehingga perlu dilakukan analisis kandungan didalam makanan olahan agar aman untuk dikonsumsi. Salah satu analisis yang dapat digunakan ialah metode imunosensor, salah satunya Enzyme-Linked Immunosorbent Assay ELISA yang memiliki tingkat sensitifias yang tinggi, mampu menguji sampel yang tidak murni, dan mampu mengikat secara selektif antigen yang dikehendaki. Metode ini memerlukan antibodi anti-gelatin babi untuk mendeteksi gelatin babi sehingga dilakukan produksi antibodi poliklonal antigen gelatin babi menggunakan hewan uji kelinci. Pada penelitian ini produksi antibodi poliklonal gelatin babi dilakukan dari antigen gelatin babi dengan mengekstraksi gelatin dari kulit babi. Rendemen yang dihasilkan sebesar 20,52 dan dikarakterisasi dengan spektrofotometer UV-Vis dan FTIR serta dianalisis dengan SDS PAGE dihasilkan bahwa gelatin babi memiliki 5 pita pemisahan dan gelatin dapat dijadikan sebagai antigen. Antibodi poliklonal antigen gelatin babi dapat diproduksi dengan hewan uji kelinci dan antibodi yang diperoleh pada hari ke 65 dilakukan pemurnian IgG. Antibodi yang dipurifikasi tersebut dapat dijadikan sebagai konjugat sensor pada imunosensor berbasis ELISA dengan konsentrasi IgG sebesar 0,289 mg/mL.

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ABSTRACTGelatin is one type of protein derived from natural collagen found in the skin and animal bones. The most widely used gelatin is pork gelatin. The use of gelatin with raw materials of pigs on food and pharmaceutical products often causes allergies, as well as not allowed in Islam, so it is necessary to analyze the content in processed foods to be safe for consumption. One of the analysis that can be used is immunosensor method, one of them is Enzyme Linked Immunosorbent Assay ELISA which has high sensitivity level, able to test impure samples, and able to selectively bind antigen desired. This method requires a pig anti gelatin antibody to detect pig gelatin so that the production of polyclonal antibody of pig gelatin antigen using rabbit test animals. In this study the production of polyclonal antigen pig gelatin carried out from pig gelatin antigen by extracting gelatin from pig skin. The yield of gelatin 20.52 and characterized by UV Vis and FTIR spectrophotometers and analyzed by SDS PAGE was found that pig gelatin has 5 separation bands and gelatin can be used as antigen. Polyclonal antibodies of antigen porcine gelatin can be produced with rabbit test animals and antibodies obtained on the 65th day of IgG purification. The purified antibodies can be used as conjugate sensors on immunosensors based ELISA with a concentration of IgG of 0.289 mg mL."

"Ester fruktosa - palmitat telah disintesis melalui reaksi esterifikasi secara enzimatis antara asam palmitat dengan fruktosa menggunakan lipase Candida rugosa E.C.3.1.1.3 terimobilisasi pada nanopartikel Fe3O4 - polidopamin. Pada penelitian ini, nanopartikel Fe3O4 - polidopamin disintesis dengan metode kopresipitasi dan selanjutnya digunakan sebagai support imobilisasi lipase. Nanopartikel Fe3O4, nanopartikel Fe3O4 - polidopamin, dan nanopartikel Fe3O4 - polidopamin - lipase telah dikarakterisasi menggunakan Fourier Transform Infra Red (FTIR), Field Emission Scanning Electron Microscopy (FESEM), Energy-Dispersive X-ray Spectroscopy (EDS), X-ray Diffraction (XRD), Vibrating Sample Magnetometer (VSM), dan Particle Size Analysis (PSA). Nilai persen loading lipase terimobilisasi pada nanopartikel Fe3O4 - polidopamin yang diperoleh adalah sebesar 99,66%. Pada reaksi esterifikasi dilakukan beberapa variasi, yaitu rasio molar fruktosa dan asam palmitat, dan pelarut. Variasi rasio molar fruktosa dan asam palmitat yang digunakan adalah 1:30, 1:60, dan 1:90 (mmol/mmol) dalam pelarut t-butanol, dan hal yang sama dilakukan dalam pelarut metil isobutil keton (MIBK). Persen konversi asam palmitat menjadi ester tertinggi diperoleh pada rasio molar fruktosa dan asam palmitat 1:30 (mmol/mmol) dalam pelarut t-butanol yaitu sekitar 28,51% pada derajat substitusi (DS) ester 2,85 dengan menggunakan lipase bebas, dan sekitar 27,75% pada DS ester 2,78 dengan menggunakan lipase terimobilisasi pada nanopartikel Fe3O4 - polidopamin.

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Fructose - palmitate ester has been synthesized via esterification reaction of palmitic acid and fructose by using immobilized enzyme of Candida rugosa E.C.3.1.1.3 lipase on Fe3O4 nanoparticles - polydopamine. In this study, Fe3O4 nanoparticles - polydopamine was synthesized by coprecipitation method and then used as support in the immobilization of lipase. Fe3O4 nanoparticles, Fe3O4 nanoparticles - polydopamine, and Fe3O4 nanoparticles - polydopamine - lipase were characterized with Fourier Transform Infra Red (FTIR), Field Emission Scanning Electron Microscopy (FESEM), Energy-Dispersive X-ray Spectroscopy (EDS), X-ray Diffraction (XRD), Vibrating Sample Magnetometer (VSM), and Particle Size Analysis (PSA). Percent value of loading immobilized lipase on Fe3O4 nanoparticles - polydopamine obtained is around 99.66%. The esterification reactions were carried out with several variations of molar ratio of fructose and palmitic acid with two different solvents. Variations molar ratio of fructose and palmitic acid used are 1:30, 1:60, and 1:90 (mmol/mmol), and the solvents used were t-butanol and methyl isobutyl ketone (MIBK). The highest percent (28,51%) conversion of palmitic acid to become ester was obtained at the molar ratio of fructose and palmitic acid 1:30 (mmol/mmol) in t-butanol with a degree of substitution (DS) ester 2,85 by using free lipase, and around 27,75% with a DS ester 2,78 by using immobilized lipase on Fe3O4 nanoparticles - polydopamine."