Judul: Pemetaan Area Prioritas Restorasi Habitat Macan Tutul Jawa (Panthera pardus melas Cuvier 1809) di Taman Nasional Gunung Halimun Salak
Abstrak: Taman Nasional Gunung Halimun Salak merupakan perluasan dari kawasan Gunung Halimun dan Gunung Salak yang juga merupakan salah satu habitat macan tutul jawa. Keberadaan spesies ini sangat rentan terhadap perubahan luasan habitat akibat deforestasi. Penelitian ini bertujuan untuk mengidentifikasi area prioritas restorasi habitat macan tutul jawa di Taman Nasional Gunung Halimun Salak. Analisis data menggunakan perangkat lunak maximum entropy dan condatis. Hasil pemodelan kesesuaian habitat digunakan untuk menentukan lokasi sumber dan target, yaitu lokasi asal dan lokasi setelah pergerakan macan tutul jawa. Hasil analisis perangkat lunak Condatis berupa nilai flow atau nilai pergerakan suatu spesies. Perubahan nilai antara skenario Bussiness As Usual dan skenario restorasi menunjukkan area yang perlu dipertimbangkan untuk restorasi. Pendugaan area prioritas restorasi kelas tinggi sebesar 3912 ha, kelas sedang sebesar 86912 ha dan kelas rendah sebesar 63464 ha. Lokasi area prioritas restorasi kelas tinggi berada pada area kebun teh Cikaniki serta beberapa area di Resort Gunung Botol, Gunung Bodas, Gunung Bedil, Kancana, Cisoka dan Cibedug berupa semak, pertanian dan pemukiman.
Keyword: condatis, kesesuaian habitat, maximum entropy

Judul: Kesesuaian Habitat Macan Tutul Jawa (Panthera pardus melas G. Cuvier) di Resort Gunung Botol Taman Nasional Gunung Halimun Salak Provinsi Jawa Barat
Abstrak: The javan’s leopard (Panthera pardus melas G. Cuvier, 1890) is a endemic carnivorous species in The Java Island. One of the Javan’s Leopard habitat is in Gunung Botol Resort Gunung Halimun Salak National Park. The research objective are mapping Javan’s Leopard habitat suitability, to identify physical factors which highly influence habitat suitability of Javan’s Leopard and to determine area of Javan’ Leopard habitat suitability. Javan’s Leopard habitat suitability mapping was initiated by collection data, such as digital map, data survey and literature. This mapping was based on some habitat variable, namely prey availability, NDVI, altitude, slope, water availability, ridge and distance from road. These variables were analyzed by using GIS and principal component analysis (PCA) to get the weight of each variable.The habitat suitability map were reclassified into three suitability class. The result showed that there were 2258.44 ha of low suitability habitat, 2801.67 ha of medium suitability habitat, 3225.84 ha of high habitat suitability and 2244.25 ha of no data. The model validation achieve 86,67% for high and medium siutability habitat.
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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.