Judul: Kajian Metoda CHAlD dan CHAlD exhaustive sebagai analisa  pohon berstruktur, Studi Kasus Frekwensi serangan Asrna pada  rnurid Sekolah Dasar Kecamatan Cipayung - Jakarta Tirnur
Abstrak: Metoda CHAlD adalah salah satu tipe metoda AID ( Automatic Interaction Detection ) yang diajukan oleh Kass (1980 ) merupakan metoda eksplorasi data yang rnenangani data kategorik. CHAlD exhaustive diajukan oleh Biggs et al (1991), mengemukakan algoritma penyekatan alternatip atas metoda CHAID atas peubah dengan jumlah kategori banyak dan peubah dengan kategori mengambang ( floating ) .
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Judul: Dampak frekuensi sel harapan yang rendah terhadap metode chaid
Abstrak: utomatic Interaction ·Detection) yang dikembangkan oleh Kass (1980), mernpakan suatu tcknik yang dapat ctigunakan untuk menelusuri struktur keterkaitan antar peubah. yaitu antara peubah respon dengan pcubah-peubah penjelas yang masing-masing merupak8.n peubah kategorik. CHAID merupakan teknik eksplorasi nonparmnetrik untuk menganalisis sekumpulan data yang besar clan berlipe kategorik. Interaksi antar peubah juga dapat dideleksi melalui melode ini (Du Toil et al .. 1986). CI-IAID banyak digunakan dalam penelitian sosial, khususnya untuk seg1ncntasi. CHAID dalam proscsnya berlandaskan pada uji khi-kuadrat yang dalam pcnggunaannya terdapal beberapa syarat yang hams terpenuhi, seperti jumlah kategori adalah tiga alau cmpat, dan minimum frckuensi sel harapan di tiap label konlingensi sama dengan 5 (Gibbons, 1985). Dalmn banyak kasus sering dijumpai bahwa fekuensi scl harapan tidak memenuhi persyaratm1 tersebut. Jika hal tersebut terjadi pada metode ini, maka akap terjadi dua proses, yaitu proses penggabungan dan proses CHAID akan berhenti (diluar anggapan bahwa prosesnya tetap akan berhenli jika semua peubah penjelas yang diamati telah dianalisis). Dalam tulisan ini, CHAID diterapkan untuk menelusuri peubah penjelas apa saja yang rnempengamhi kepernilikan ATM, yang dalam kasus ini didapatkan bahwa status bank mcmpengaruhi kepcmilikan ATM.
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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