Judul: Perencanaan Tapak Bumi Perkemahan Kawasan Wisata Alam Gunung Tujuh Taman Nasional Kerinci Seblat Kabupaten Kerinci, Jambi
Abstrak: Taman Nasional Kerinci Seblat (TNKS) merupakan Taman Nasional terbesar kedua di Indonesia setelah Taman Nasional Lorentz. Luas TNKS meliputi 1 484 650 ha yang tersebar di 4 propinsi yaitu Jambi, Sumatera Barat, Bengkulu dan Sumatera Selatan. Hingga saat ini, upaya untuk memperkenalkan TNKS belum banyak dilakukan. Salah satu cara untuk lebih memperkenalkan TNKS adalah dengan mengembangkan zona pemanfaatan yang terletak di Resort Gunung Tujuh menjadi kawasan wisata alam.
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Judul: Perencanaan Lanskap Areal Wisata Alam Gunung Tujuh, Taman Nasional Kerinci Seblat, Propinsi Jambi
Abstrak: Indonesia terkenal dengan kekayaan sumberdaya alamnya. Salah satu sumberdaya alam Indonesia yang mempunyai potensi untuk dikembangkan, adalah Taman Nasional. Taman Nasional Kerinci Seblat (TNKS) adalah salah satu dari 34 Taman Nasional yang ada di Indonesia, dan merupakan Taman Nasional yang terluas dan terpenting di Asia (MacKinnon dan MacKinnon, 1986). Salah satu pemanfaatan yang ekonomis dari suatu taman nasional adalah sebagai kawasan wisata, sehingga diperlukan suatu perencanaan yang baik untuk mengoptimalkan bahkan memaksimalkan pemanfaatannya.
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Judul: Pemurnian dan karakterisasi protein inhibitor RNA helikase virus hepatitis C
Abstrak: Hepatitis C virus (HCV) infection is the second most common chronic viral infection in the world with global prevalence. This infection is contribution to chronic hepatitis and liver cirrhosis, often leading to hepatocellular carcinoma. There is no effective drug and vaccine available against HCV. The current standard treatment, a combination of pegylated interferon-α with ribavirin, is limited by its suboptimal response rate in a significant patient population, side effects, and affordability. Therefore, development of effective drug is needed. One approach to find out the candidate of antiviral drug is to discover the inhibitor of enzyme that essential for virus replication, such as RNA helicase. Streptomyces chartreusis 5-095 produce the inhibitor of HCV RNA helicase. The aim of this study was to purify the protein inhibitor which has inhibition activity against ATPase activity of RNA helicase HCV from S. chartreusis 5-095. The supernatant of culture S. chartreusis 5-095 exhibited high inhibiton activity against ATPase activity of RNA helicase HCV (approximately 72%) at 10 days of incubation. The extracellular protein inhibitor was partially purified by procedures of precipitation with ammonium sulfate to 65% saturation and gel filtration (Sephadex G50) using methanol water solution (4:6) as an eluen. The purity of protein inhibitor was monitored by SDS PAGE. The protein inhibitor showed a relative molecular mass were estimated to be 14 kDa and increased the purity 23,08 fold than those of the crude protein. The specific activity and IC50 after purification were 13,1338 U/mg and 0,0767 mg/mL, respectively. The activity of purified protein inhibitor showed its stability over pH range from 5-8 and optimum at pH 7,4. The inhibition activity showed its stability up to 70% at temperature 100 oC. The purified protein inhibitor relatively stable its activity at storage in the range of -20 oC to room temperature for 35 days.
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