Judul: Dinamika kehidupan anak jalanan di rumah singgah : studi kasus anak-anak jalanan di rumah singgah kasih sayang, Cempaka Putih Barat-Jakarta Pusat
Abstrak: Tujuan dari penelitian ini adalah untuk mengetahui tentang peran rumah singgah bagi anak-anak jalanan, mengetahui pembinaan apa saja yang dilakukan oleh rumah singgah bagi anak jalanan, serta bagaimana manfaat pembinaan tersebut bagi mereka. Metode penelitian yang digunakan adalah metode penelitian kualitatif dengan menggunakan teknik wawancara mendalam serta pengumpulan data sekunder. Dipilihnya rumah singgah ini sebagai lokasi penelitian karena rumah singgah ini merupakan salah satu rumah singgah pertama yang dibentuk oleh Departemen Sosial sebagai proyek percontohan, khususnya untuk wilayah Jakarta Pusat.
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Judul: Analisis peranan rumah singgah dalam upaya perlindungan anak jalanan kasus rumah singgah kita, Kelurahan Gunung, Kecamatan Bogor Barat, Kabupaten Bogor, Propinsi Jawa Barat
Abstrak: Krisis moneter yang melanda Indonesia beberapa tahun silam membawa dampak yang sangat berarti bagi kehidupan masyarakat Indonesia di segala bidang, terutama di bidang sosial ekonomi yang ditandai dengan meningkatnya jumlah penduduk miskin. Hal ini merupakan salah satu hal yang menyebabkan tingginya fenomena anak jalanan di perkotaan. Kehidupan jalanan yang rawan akan kekerasan baik dalam bentuk fisik, psikologis dan seksual tentu saja membuat kita merasa iba. Oleh karena itu anak jalanan sangat membutuhkan perlindungan. Salah satu upaya perlindungan dapat dilakukan melalui pemenuhan kebutuhan (sandang, pangan, papan, pendidikan, kasih sayang, dan kesehatan) yang dilakukan oleh rumah singgah.
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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