Judul: Perbandingan Metode Diskretisasi Data  Partisi Intuitif dan K-Means Clustering  terhadap Pembuatan Pohon Keputusan
Abstrak: Data sektor pertanian yang dimiliki Departemen Pertanian selalu bertambah setiap tahun sehingga menghasilkan sekumpulan data berukuran besar. Data tesebut mengandung informasi yang masih harus ditambang. Dalam penelitian ini, dibandingkan hasil pembentukan pohon keputusan menggunakan algoritme ID3 dengan metode diskretisasi Partisi Intuitif dan algoritme K-Means Clustering dengan jumlah cluster 4 dan 5 cluster Pohon keputusan dibentuk menggunakan algoritme ID3 yang sudah tersedia dalam perangkat lunak WEKA (Waikato Environment Knowledge Analysis). Berdasarkan keluaran dari WEKA, aturan yang dihasilkan oleh metode Partisi Intuitif berjumlah 63 dengan akurasi sebesar 84,54%. Aturan yang dihasilkan oleh algoritme K-Means clustering dengan 4 cluster berjumlah 49 dengan akurasi sebesar 87.40% dan aturan yang dihasilkan menggunakan algoritme K-Means clustering dengan jumlah cluster 5 berjumlah 59 dengan akurasi sebesar 76.87%. Nilai Root Means Square Error (RMSE) yang dihasilkan oleh masing masing metode yaitu Partisi Intuitif sebesar 0.12, algoritme K-Means clustering dengan jumlah cluster 4 sebesar 0.2 dan algoritme KMeans clustering dengan jumlah cluster 5 sebesar 0.24. Nilai RMSE dari hasil percobaan menunjukkan bahwa hasil terbaik terdapat pada pohon keputusan yang dibentuk dengan metode diskretisasi data partisi intuitif.
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Judul: Penerapan teknik klasifikasi dengan algoritme decision tree untuk data tanaman pangan dan hortikultura
Abstrak: Data sektor pertanian yang dimiliki oleh Departemen Pertanian selalu bertambah setiap tahun sehingga menghasilkan kumpulan data berukuran besar. Data tersebut terdiri dari 18 subsektor dan 16 atribut, termasuk di dalamnya data subsektor tanaman pangan dan hortikultura. Data tanaman pangan dan hortikultura terdi ri dari 109.037 record. Dalam penelitian yang telah dilakukan, diaplikasikan salah satu teknik data mining, yaitu klasifikasi dengan menggunakan algoritma decision tree, untuk melihat pola yang ada dalam data tanaman pangan dan hortikultura. Decision tree merupakan algoritma dalam klasifikasi yang paling banyak digunakan. Algoritma ini terdiri dari 3 (tiga) tahapan, yaitu pembentukan pohon; pemangkasan pohon; dan pembentukan aturan (IF-AND-THEN). Data tanaman pangan dan hortikultura dibagi menjadi 8 data set berdasarkan kelompok tahun yang terbagi per lima tahun, yaitu bdspT1 sampai dengan bdspT8, yang masing-masing terdiri dari atribut komoditas; lokasi; produktivitas; dan luas panen. Setiap data set tersebut dibagi menjadi 75% training set dan 25% test set.
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Judul: Extracellular Expression of thermostable Geobacillus stearothermophilus T1.2RQ Lipase for Biodiesel Production
Abstrak: The extracellular expression of enzymes in an excellent secretion host such as Bacillus subtilis is a useful strategy for making enzymes of industrial significance more affordable by lowering the cost of its downstream processing. Lipases are a category of hydrolases that catalyze the hydrolysis of triglycerides to glycerol and free fatty acids. Also, lipases catalyze the hydrolysis and transesterification of other esters as well as the synthesis of esters. They can perform very specific biotransformation reactions and are widely used in food, organic synthesis, detergents, cosmetic, and pharmaceutical industries. Geobacillus stearothermophilus T1.2RQ lipase is an industrially-desired thermostable lipolytic enzyme with an excellent hydrolytic and transesterification activity. This study aimed to express T1.2RQ lipase, in B. subtilis WB800 and ensure its secretion into the extracellular medium. Three signal peptides (AmyQ, Epr, LipA) and two promoters (Pgrac01 and Pgrac100) were used in the secretory-expression of T1.2RQ lipase, based on five constructed expression vectors constructed by restriction cloning and PCR mutagenesis. Sangers sequencing was used to verify constructs to ensure they are in the correct reading frame. Recombinants vectors, pHT43 (plasmid control), pHT43-T1.2RQ, pHT43- T1.2RQ_AmyQ, pHT43-T1.2RQ_Epr, and pHT43-T1.2RQ_LipA, were transformed by electroporation into Bacillus subtilis WB800. The electroporation was successful with the optimum condition of 2500V, 200 ohms, 25µF, and 5milliseconds. Recombinant B. subtilis pHT43 (negative control) and pHT43-T1.2RQlip + signal peptides were streaked on the lipidic agar, LA+TBN. All four recombinants, including the negative control (B. subtilis WB800-pHT43), produced clear zones on the TBN agar plate after overnight incubation (fig 2), indicating the presence of a lipolytic enzyme in all of the recombinant B. subtilis cells. pHT43-T1.2RQlip + signal peptides (AmyQ, Epr, and LipA) have clear zones with significantly higher diameters than B. subtilis WB800-pHT43 (negative control). This phenomenon suggests that the recombinant thermostable lipase T1.2RQ introduced into these cells was successfully expressed, thereby increasing the lipolytic capability of its host cells T1.2RQ lipase was expressed in 50ml terrific broth medium (TB) and the expression induced with 1mM IPTG. Lipase activity assay using p-nitrophenyl esters showed that all three signal peptides directed the secretion of T1.2RQ lipase into the extracellular medium. Signal peptide, LipA, resulted in the highest extracellular activity of 5.6 U/mL, which corresponds to a 6-fold increase over the parent B. subtilis WB800 strain. Meanwhile, signal peptides, AmyQ and Epr produced 4.2 U/mL and 3.4 U/mL activity respectively. SDS-Zymogram analysis confirmed that T1.2RQ lipase was correctly processed and secreted in its original size of 44 kDa. An attempt to further increase lipase expression level by promoter optimization showed that, contrary to expectation, promoter Pgrac100 exhibited similar expression levels as the original Pgrac01. Nevertheless, the demonstration of the successful secretion of T1.2RQ lipase in this work confirms the latter as a promising approach for the industrial production of the enzyme
Keyword: Bacillus subtilis, Expression, Extracellular, Heterologous, Lipase, Thermostable