Judul: Analisis Perilaku Pasien dalam Memilih Klinik  Kesehatan di Depok
Abstrak: Klinik kesehatan merupakan salah satu jenis usaha kecil menengah yang saat ini berkembang cukup pesat di kota Depok. Bila pada tahun 2002 hanya terdapat sebanyak 18 klinik kesehatan di kota Depok, maka di tahun 2007 telah berdiri sebanyak 142 klinik kesehatan. Perkembangan jumlah klinik kesehatan ini tidak terlepas dari perkembangan jumlah penduduk kota Depok, yang pada tahun 2007 berjumlah sebanyak 1,4 juta penduduk. Pesatnya pertumbuhan usaha tersebut menyebabkan terjadinya persaingan antara klinik kesehatan, dimana akibat dari persaingan tersebut dan seperti usaha lainnya, terdapat klinik kesehatan yang ramai dan berkembang, tetapi terdapat juga yang sepi, padahal beberapa diantaranya memberikan jenis pelayanan kesehatan yang sama dan berada di lokasi yang berdekatan.
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Judul: Analisis Tingkat Kepuasan Pasien Rawat Jalan Terhadap Kualitas Pelayanan (Studi Kasus: Rumah Sakit Pusat Pertamina)
Abstrak: Sejak dikeluarkannya Pakto 88 yang memperbolehkan investor swasta untuk menanamkan investasinya pada beberapa industri jasa di Indonesia mendorong terjadinya peningkatan jumlah pendirian rumah sakit yang semakin pesat. Hal ini dapat diartikan bahwa kuantitas pesaing semakin bertambah dan persaingan semakin ketat terutama pada rumah sakit swasta. Pemberian pelayanan dengan kualitas tinggi menjadi hal yang harus diutamakan dalam suatu rumah sakit karena pada dasarnya kinerja pelayanan inilah yang dijual ke masyarakat dan dapat mempengaruhi kepuasan. Rumah Sakit Pusat Pertamina (RSPP) mempunyai misi untuk mencapai loyalitas dengan kepuasan pelanggan dan menggalakkan program yang bernama Service Year pada tahun 2003 lalu. Terdapat dua hal yang perlu segera diperbaiki pada instalasi rawat jalan dalam program tersebut yaitu: (1) perbaikan dalam menunggu konsultasi dokter dan antri obat di apotik dan (2) perbaikan pada bagian pendaftaran pasien dan pembayaran di kasir.
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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