Judul: Studi komposisi jenis dan struktur komunitas tumbuhan dalam sistem agroforestry kawasan cagar budaya dan buah-buahan condet
Abstrak: Penduduk yang berjumlah besar dengan daya dukung ta- nah yang rendah, tingkat pertumbuhan penduduk yang cepat bersamaan dengan tingkat kerusakan lingkungan yang cepat dan desakan pertumbuhan ekonomi, merupakan beberapa masa- lah yang dihadapi kota besar seperti Jakarta. Daerah Condet yang terletak di Kecamatan Kramat Jati Jakarta Timur, telah ditetapkan oleh pemerintah melalui SK Gubernur KDKI No. D-I. 7903/a/30/75 sebagai kawasan Cagar Budaya dan Buah-buahan. Diduga dengan semakin pesatnya program pembangunan yang ada pada saat ini, telah terjadi perubahan terhadap daerah Condet, terutama terhadap komposisi jenis dan struktur komunitas tumbuhan dalam sistem Agroforestry daerah Condet. Komposisi jenis diperoleh dengan cara mencacah dan mengidentifikasi pohon. Struktur komunitas tumbuhan diperoleh dengan analisis profil arsitektur komunitas tumbuhan. Masing-masing pada daerah di sekitar sungai Ciliwung Kelurahan Bale Kambang (daerah A) dan di Kelu- rahan Kampung Tengah (daerah B)....
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Judul: Agrotourism Landscape Design of Cagar Buah Condet in East Jakarta
Abstrak: Laju pertambahan penduduk DKI Jakarta yang semakin cepat mengakibatkan sejumlah dampak negatif. Salah satunya adalah peningkatan laju alih fungsi lahan menjadi permukiman. Secara spesifik, alih fungsi lahan di Jakarta Timur mengakibatkan buah-buah lokal terancam punah termasuk salak condet yang merupakan maskot dari DKI Jakarta. Oleh karena itu, penting untuk meneliti upaya pengembangan dan pelestarian buah-buah lokal melalui penataan lanskap agrowisata. Tapak yang berpotensi dikembangkan adalah Cagar Buah Condet. Tapak ini dijadikan tempat pelestarian buah-buah lokal. Penelitian ini bertujuan mengidentifikasi dan membuat analisis-sintesis kondisi tapak berdasarkan potensi dan kendala, menentukan konsep agrowisata dan konsep desain lanskap agrowisata, serta merancang lanskap agrowisata Cagar Buah Condet. Metode penelitian ini menggunakan analisis spasial untuk mengolah aspek fisik dan biofisik, analisis deskriptif kuantitatif untuk menghitung Thermal Humadity Index, daya dukung fisik, dan penilaian kriteria kelayakan agrowisata, serta analisis deskriptif kualitatif untuk mengetahui preferensi pengguna. Konsep dasar yang diterapkan adalah “Centeng Barengan”, sedangkan konsep desain mengabstraksi bentuk kembang kelapa khas Betawi seperti pada pola tapak, pola perkerasan, dan desain elemen keras. Desain tapak ditujukan untuk memberikan ruang interaksi antara pengunjung dan alam dengan mengoptimalkan daya tarik pertanian yang tersedia.
Keyword: Agrotourism, Condet, Local Fruit

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