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.
Keyword: 

Judul: Keanekaragaman Jenis Burung pada Beberapa Tipe Habitat di Hutan Harapan, Sumatera.
Abstrak: Gangguan habitat dapat menyebabkan terbentuknya beberapa habitat yang berbeda di kawasan Hutan Harapan diantaranya habitat tanah terbuka, belukar muda, belukar tua, dan hutan kering sekunder. Penelitian ini bertujuan untuk mengidentifikasi keanekaragaman burung pada tipe habitat yang berbeda, mendeskripsikan keempat tipe habitat, dan mengidentifikasi komposisi guild burung. Penelitian ini dilakukan pada bulan Mei hingga Juni 2017 pada empat tipe habitat di kawasan Hutan Harapan Sumatera dengan menggunakan metode MacKinnon dan metode titik hitung atau IPA (Indices Ponctuel d’Abondance). Dalam penelitian ini ditemukan burung sebanyak 84 jenis dari 33 famili. Jumlah jenis burung paling banyak yaitu di habitat belukar tua sebanyak 50 jenis burung dengan indeks keanekaragaman (H’) sebesar 3.42, habitat hutan kering sekunder ditemukan 42 jenis (H’=3.41), habitat belukar muda sebanyak 26 jenis burung (H’=2.64), dan habitat tanah terbuka sebanyak 20 jenis burung (H’=2.36). Kesamaan komunitas burung tertinggi yaitu pada habitat belukar tua dan hutan kering sekunder yaitu 0.61. Komposisi burung berdasarkan guild tertinggi yaitu burung pemakan serangga.
Keyword: habitat, keanekaragaman, burung, MacKinnon, IPA

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