Judul: Keanekaragaman jenis burung pada beberapa tipe habitat di areal hutan lindung KPH Madiun perum perhutani unit II Jawa Timur
Abstrak: The objectives of this study are: (1) to make a list of bird species at several types of habitats, (2) to compare birds species diversity at several types of habitat, and (3) to examine factors that influence birds species in the study area. The research was done in four types of habitats in the protected forest area of Kesatuan Pemangkuan Hutan (KPH) Madiun, namely, natural forest, mahogany forest (Swietenia macrophylla), take forest (Tectona grandis) and sonobrit forest (Dalbergia sisso) from June to August 2007.
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Judul: Keanekaragaman jenis Burung pada beberapa tipe Habitat di Hutan Penelitian Dramaga, Bogor, Jawa Barat
Abstrak: Dramaga Research Forest, located in the outskirt of Bogor, provides a good habitat for birds. This research was aimed to study bird diversity, identifying habitat characteristics (around the forest path, along house edge, riparian habitat and the interior area) and recorded the activities of the local people around the forest. Point count, MacKinnon list, habitat profiling and interviews were conducted. Shannon-Wiener diversity indices and similarity level were calculated. The highest index of species diversity was in the interior area (2.34), followed by around the forest path (2.21), along house edge (1.97) and riparian habitat (1.86). The highest species richness, however, was in the riparian habitat (27 species), the forest path had 21 species, along house edge had 26 species, while the interior area was a home for 21 bird species. The highest similarity (0.81) was between forest path and interior area. On the activities of the local people, the most often was firewood harvesting. Other activities were hunting for cage birds, harvesting ferns, harvesting wild fruit and harvesting ant larvae. Activity that might disrupt the bird population was hunting.
Keyword: Bogor Agricultural University (IPB), Dramaga research forest, human activities, Bird diversity, Streptopelia chinensis, Orthotomus sepium

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