Judul: Prioritas Pengembangan Hutan Kota di Jakarta Selatan
Abstrak: South Jakarta is one of the densely populated municipality in DKI Jakarta. Increased urbanization causes degraded lands green space that will lead to environmental degradation such as air pollution and rising temperatures. Urban forest is one of green space that is capable of restoring the balance and healthy urban environment. Criteria in the selection of priority areas using the variable surface temperature and air pollutants and classified by three classes of priority. Urban forest priority location is the availability of green space that goes into the priority class . The results of this study indicate priority areas in the first class of 1269.86 ha ( 8.72 % ) , the second class of 7076.55 ha ( 48.61 % ) and the third class of 6210.03 ha ( 42.66 % ) . The availability of green space that was in the first priority class of 77.96 Ha , the second class of 327.57 Ha and class of 983.61 Ha . Total green space can not be found to reach 10 % of the South Jakarta areas because land limitation and convertion land use.
Keyword: surface temperature., urban forest, temperature, priority location, green space, air pollutants

Judul: Penentuan Lokasi Pengembangan Ruang Terbuka Hijau Berdasarkan Sebaran Suhu Permukaan Di Kotamadya Jakarta Barat
Abstrak: Pesatnya pembangunan cenderung mengorbankan bentang alam hijau serta mengabaikan pentingnya Ruang Terbuka Hijau (RTH) bagi kota. Minimnya RTH menyebabkan berkurangnya kemampuan kota dalam menurunkan suhu permukaan. Kotamadya Jakarta Barat merupakan salah satu kotamadya di DKI Jakarta, yang mengelola RTH terendah. Penelitian ini dilakukan untuk menentukan lokasi pengembangan RTH berdasarkan sebaran suhu permukaan dalam upaya mengurangi suhu permukaan dan menciptakan lingkungan yang nyaman dan sehat. Penentuan lokasi pengembangan RTH menggunakan kelas prioritas, dengan pertimbangan sebaran suhu permukaan dan digolongkan menjadi tiga kelas prioritas. Hasil penelitian menunjukkan bahwa kelas prioritas pertama seluas 2 591 ha, kedua seluas 6 961 ha, dan ketiga seluas 3 072 ha. Jumlah luasan RTH di kelas prioritas pertama yang dapat dikembangkan sebesar 20 ha pada RTH pohon dan 54 ha pada RTH non pohon.
Keyword: kelas prioritas, lingkungan, ruang terbuka hijau, suhu permukaan

Judul: Heterologous Expression Of Endo-Β-Xylanase From Bacillus Pumilus Strain Bcrs-01 In Escherichia Coli.
Abstrak: Xylanases are glycoside hydrolase family 11 which depolymerise xylan in the plant cell wall, the most excessive form of hemicellulose. Endo-β-xylanases (EC 3.2.1.8) are most important to breakdown β-1,4-glicoside bond of xylan to produce disaccaride xyloolygosaccaride (XOs) and xylose (monomer). Bovine rumen fluids have potential to obtain endo-β-xylanase produced of bacteria. The objectives of this study were to obtain xylanase producing bacteria and to express xynA gene encoding endo-β-xylanase from bacterium in Escherichia coli. Twenty nine isolate bacteria have been succesfully isolated from bovine rumen fluid in agar medium containing birchwood xylan. Isolate BCRS-01 bacterium was previously screened for the high production of xylanase. Based on 16S rRNA gene sequence analysis, BCRS-01 showed high similarity (99%) to Bacillus pumilus (accession number NR043241). The crude xylanase had optimal activity at 55oC, pH 7.0. Furthermore, the crude xylanase exhibited broad pH stability from 4.0 to 10.0 and remained more than 60% and 40% of its activity after incubation at pH 4.0 until 10.0, respectively for 60 min. It also showed a stability at temperature 25-50oC since it retained 80% and 50% of its activity when incubated at 50oC or 30 and 60 min, respectively. The xylanase activity was strongly inhibited by Ca2+ and Cu2+ at concentration 10 mM, and as little as 1 mM for Mn2+. Therefore, this xylanase has potentially used as additive feeds in animal feed industry. The DNA sequence xynA gene encoded endo-β-xylanase was amplified and cloned into the expression vector pET-15by under the control of T7 promoter. The recombinant protein had succesfully expressed in Escherichia coli BL21 (DE3) pLysS. A protein recombinant of approximately, 26.7 kDa was observed on the SDS-PAGE analysis. Crude extract of recombinant endo-β-xylanase demonstrated activity of enzyme at 56 U mL-1 using birchwood xylan as a substrate at 55oC for 10 min.
Keyword: Bacillus pumilus, bovine rumen fluid, endo-β-xylanase, heterologous expression.