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.
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Judul: Pemanfaatan Habitat oleh Burung Air di Taman Wisata Alam Angke Kapuk Jakarta
Abstrak: Taman Wisata Alam Angke Kapuk adalah salah satu kawasan lahan basah di Jakarta yang menjadi habitat burung air. Penelitian ini bertujuan mendeskripsikan habitat, mengidentifikasi jenis, dan menjelaskan pemanfaatan habitat serta faktor yang mempengaruhi pemanfaatan habitat oleh burung air di Taman Wisata Alam Angke Kapuk. Pengambilan data dilakukan dengan transek dan metode scan sampling. Pengamatan dilakukan pagi, siang, dan sore hari dengan 3 kali pengulangan masing-masing habitat. Habitat dibagi menjadi hutan mangrove, danau, muara sungai, dan rawa. Jumlah spesies yang ditemukan di habitat hutan mangrove 10 spesies, danau 13 spesies, muara sungai 14 spesies, dan rawa 7 spesies. Habitat danau dimanfaatkan untuk makan (48%). Habitat hutan mangrove dimanfaatkan untuk beristirahat (30%) dan waspada (16%). Habitat muara sungai dimanfaatkan untuk merawat tubuh (22%) dan berpindah (18%). Habitat rawa dimanfaatkan untuk istirahat (36%) dan menyerang (8%). Faktor yang mempengaruhi pemanfaatan habitat oleh burung air yaitu perburuan liar, aktivitas rekreasi, aktivitas nelayan, pengalihfungsian lahan, dan pencurian ikan.
Keyword: community common, threat to waterbirds, water bird activity

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