Judul: Capm (The Capital Assets Pricing Model) N-Momen Pada Asuransi Bencana
Abstrak: Skewness adalah ukuran penyimpangan yang terjadi pada nilai dari sebaran imbal hasil. Skewness dalam suatu nilai pada sebaran imbal hasil menyebabkan terjadinya ketidakseimbangan pada nilai premi, imbal hasil, dan risiko. Contoh nyata dari sebaran yang mengalami penyimpangan adalah nilai imbal hasil perusahaan asuransi bencana. Bencana yang bersifat acak dan langka menyebabkan nilai dari sebaran imbal hasil perusahaan asuransi bencana mengalami penyimpangan dan menyebar asimetris, sehingga diperlukan suatu model penduga risiko dan imbal hasil yang menyebar asimetris.
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Judul: Pemilihan Portofolio Dan Pembentukan Harga Aset – Kerangka  Kerja Tiga-Parameter
Abstrak: Capital Asset Pricing Model (CAPM) merupakan alat untuk memprediksi keseimbangan imbal hasil yang diharapkan dari suatu aset berisiko. CAPM diasumsikan menyebar normal untuk rataan dan ragamnya. Namun dalam kenyataannya, sering terjadi penyimpangan terhadap imbal hasil yang diharapkan. Untuk itu diperlukan pengembangan model CAPM dua parameter menjadi CAPM tiga parameter. Momen ketiga, yaitu kecondongan dari suatu aset berisiko digunakan untuk CAPM tiga parameter. Kecondongan merupakan alat untuk mengukur sebaran asimetris yang terjadi akibat penyimpangan tersebut. Untuk melakukan investasi, para investor dapat memilih sekuritas-sekuritas yang ada sehingga membentuk portofolio yang optimal. Portofolio dengan tiga parameter, yaitu rataan, ragam, dan kecondongan memperbolehkan pembatasan terhadap short sales. Jika portofolio tidak optimal, maka dapat menggunakan model CAPM tiga parameter. Dalam tulisan ini akan ditelaah ulang pembentukan harga pasar aset dengan menggunakan tiga parameter. Masalah pembentukan harga ini dapat diselesaikan dengan menggunakan model CAPM tiga parameter yang melibatkan kecondongan dari imbal hasil aset berisiko.
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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