Judul: Hubungan Komponen Habitat Suaka Margasatwa  Muara Angke Dan Hutan Lindung Angke Kapuk  Dengan Burung Air
Abstrak: Keberadaan burung air dalam suatu kawasan memiliki hubungan dengan komponen-kornponen pembentuk habitat. Dalam penelitian ini dipelajari hubungan beserta sebaran burung air di Suaka Margasatwa Muara Angke dan Hutan Lindung Angke Kapuk pada bagian tambak. Komponen-komponen habitat yang diukur pada setiap titik pengamatan adalah, banyaknya jenis tumbuhan, banyaknya jenis dan individu pohon dengan tinggi diatas dan dibawah 3 m, Gosentase penutupan tajuk pohon, prosentase penutupan tumbuhan bawah dan prosentase perairan terbuka, dan profil vertikal dari plot contoh yaitu banyaknya lapisan tajuk, pohon tertinggi, terendah dan rata-rata tinggi pohon berdiameter diatas dan dibawah 12 cm, rata-rata tinggi tumbuhan bawah dan tinggi bertenggernya burung air, yang mempengaruhinya.
Keyword: 

Judul: Kajian karakteristik kawasan hutan Angke-Kapuk untuk pembinaan habitat burung air sebagai penunjang kegiaatan wisata di DKI Jakarta
Abstrak: Perkembangan suatu kota dan meningkatnya berbagai aktivitas manusia, menyebabkan kondisi lingkungan di dalam maupun di luar kawasan konservasi telah mengalami banyak perubahan. Salah satu kawasan konservasi yang semakin menyempit adalah Kawasan Hutan Angke-Kapuk, termasuk didalamnya Cagar Alam Muara Angke, Hutan Wisata Muara Kamal dan Hutan Lindung. Kawasan ini telah mengalami perubahan dengan adanya pembangunan pemukiman Pantai Indah Kapuk yang mereklamasikan tanah rawa menjadi kawasan pemukiman. Dari beberapa penelitian terdahulu, diketahui bahwa Kawasan Hutan Angke- Kapuk yang terletak di wilayah perkotaan (Jakarta) merupakan habitat bagi burung- burung air. (Avenzora, 1988 dan Nainggolan, 1994). Dalam kaitannya dengan pembinaan habitat dan Bird watching, wilayah perkotaan sesungguhnya dapat dibina untuk melestarikan burung. Untuk menunjang upaya pelestarian burung serta meningkatkan rasa memiliki terhadap burung, khususnya burung-burung air, diadakan suatu penelitian di Kawasan Hutan Angke-Kapuk, yang meliputi Cagar Alam Muara Angke, Perumahan Pantai Indah Kapuk dan Hutan Wisata Kamal. Penelitian ini bertujuan untuk mengetahui aspek ekologis kehidupan burung air (keanekaragaman, kelimpahan, komposisi, penyebaran, penggunaan habitat), kondisi komponen habitat burung air (komposisi dan struktur vegetasi, ketersediaan pakan, tempat bersarang dan tempat beristirahat) dan kondisi kawasan sebagai habitat burung air. Diharapkan penelitian ini dapat memberikan bahan pertimbangan bagi pemerintah DKI dan Sub BKSDA DKI Jakarta sebagai perencana kawasan dalam menentukan langkah kebijaksanaan dalam pengelolaannya, dalam hal ini kaitannya sebagai tempat kegiatan wisata.
Keyword: 

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