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Abstrak :
Studi tentang biotransformasi asetonitril menggunakan bakteri Gram positif yang diisolasi dari sedimen sungai yang sudah tercemar limbah industri di kawasan Cibinong, Jawa Barat telah dilakukan. Sebanyak 200 isolat bakteri telah diskrining aktivitasnya dalam mendegradasi senyawa nitril, dan didapatkan 2 isolat unggulan yaitu isolat 100A dan 100D. Hasil skrining pada medium mineral yang mengandung asetonitril dengan konsentrasi 100 mM, menunjukkan indikasi kuat bahwa bakteri tersebut mampu menghasilkan enzim nitril hidratase dan amidase. Akan tetapi, kedua bakteri tersebut tidak mampu tumbuh pada media yang mengandung benzonitril. Hasil ini didukung dengan data karakterisasi secara molekuler dengan menggunakan primer spesifik, dimana isolat 100A dan 100D secara positif mengandung gen penyandi α-nitril hidratase dan amidase. Pada posisi pertama susunan asam amino dari gen penyandi α-nitril hidratase terdapat perbedaan antara isolat 100A (Methionine 1) dan 100D (Glycine 1). Hasil identifikasi berdasarkan analisis filogenetik menggunakan sekuen 16S ribosomal DNA menunjukkan bahwa kedua bakteri ini memiliki kekerabatan yang sangat dekat dengan Rhodococcus qingshengii, R. baikonurensis dan R. erythropolis. Analisis pairwise nucleotide alignment menunjukkan bakteri 100A dan 100D memiliki susunan nukleotida yang lebih mirip dengan R. qingshengii, sehingga kedua isolat bakteri tersebut diberi nama Rhodococcus aff. qingshengii 100A dan Rhodococcus aff. qingshengii 100D. ...... Study of the biotransformation of acetonitrile using Gram-positive bacteria isolated from sediment of industrial waste contaminated river in Cibinong, West Java has been carried out. A total of 200 bacterial isolates were screened for their activity in degrading nitrile compounds of which two isolates with highest activity were selected for the molecular characterization. Screening of nitrile degrading enzymes using mineral medium 100 mM acetonitrile showed that isolates 100A and 100D capable of producing α-nitrile hidratase and amidase enzymes. However, both bacteria are unable to grow on media containing benzonitrile. These results were supported by molecular characterization using specific primers, where isolates100A and 100D positively contain genes encoding α-nitrile hidratase and amidase. There was a difference at the first position of amino acid composition of the gene encoding α-nitrile hidratase between isolates 100A (Methionine1) and 100D (Glycine1). Identification based on phylogenetic analysis using 16S ribosomal DNA sequences showed that the two bacteria have a very close relationship with Rhodococcus qingshengii, R. baikonurensis and R. erythropolis. Based on the analyses using pairwise nucleotide alignment, the nucleotide sequences of strain 100A and 100D more similar to R. qingshengii, therefore, these bacteria were named Rhodococcus aff. qingshengii 100A and Rhodococcus aff. qingshengii 100D.

Abstrak :
Telah dilakukan pengembangan metode pemurnian hyaluronidase testis sapi Bali menggunakan teknik pemisahan kromatografi afinitas. Hyaluronidase testiskular (E.C.3.2.1.35) adalah enzim yang dapat menghidrolisis asam hyaluronat. Hyaluronidase dari testis sapi Bali difraksionasi dengan amonium sulfat, setelah dialisis dilakukan pemurnian menggunakan kolom kromatografi afinitas sepharose blue CL-6B, diperoleh aktivitas spesifik sebesar 102,93x10-3 U/mg dengan tingkat pemurnian 53,70 kali dan rendemen 64,24 % dari ekstrak kasar. Fraksi sepharose blue CL-6B yang diperoleh dimurnikan lebih lanjut dengan kolom imunoafinitas CNBr-activated Sepharose 4 FF dengan imunoglobulin G spesifik hyaluronidase (IgG diperoleh dari imunisasi kelinci dewasa dengan standar hyaluronidase) diperoleh aktivitas spesifik 705,89 x 10-3 U/mg dengan tingkat pemurnian 388,86 kali dan rendemen 38,62 %. Pemurnian hyaluronidase dari fraksi sepharose blue CL-6B yang dilanjutkan dengan kromatografi penukar ion DEAE FF memiliki aktivitas spesifik 307,65 x 10-3 U/mg, tingkat pemurnian 169,49 kali dan rendemen 48,66 % dari ekstrak kasar. Dengan elektroforesis gel SDS-PAGE diperkirakan bobot molekul hyaluronidase testis sapi Bali 61, 52 kDa. Dalam larutan dapar glisin aktivitas enzim optimum pada pH 5,0. Hyaluronidase dalam fraksi pemurnian relatif stabil bila disimpan pada suhu 0 oC dibanding pada suhu 4 oC dan 25 oC., setelah 12 hari penyimpanan fraksi pemurnian enzim mengalami penurunan aktivitas sebesar 41,51% (ekstrak kasar), 34,63 % (fraksi amonium sulfat) dan 37,42 % (dialisis). ......Testicular hyaluronidase (E.C.3.2.1.35) is an enzyme that hydrolyzes hyaluronic acid. Extracted Hyaluronidase from Bali bovine testis was fractionated by ammonium sulphate followed by dialysis and purification over affinity chromatography on sepharose blue CL-6B. Spesific activity of purified hyaluronidase was 102,93 x 10–3 U/mg with 53,70-fold purification and yielded 64,24 % as to the original crude extract. The fractionated sepharose blue CL-6B was chromatographied by CNBr activated sepharose 4FF which was coupled with rabbit immunoglobulin (IgG) spesific to hyaluronidase. Spesific activity of purified enzyme was 705,89 x 10-3 U/mg with 388,86-fold purification and yield 38,62 %. Purification of the fractionated sepharose blue CL-6B by ion exchanger chromatography produced the purified enzyme with spesific activity 307,65 x 10-3 U/mg, purification 169,49-fold and yield 48,66 %. The molecular weight of hyaluronidase isolated from Bali bovine testis estimated by SDS-PAGE was 61,52 kDa. The optimum hydrolytic activity of enzyme in glysine buffer was on pH 5,0. The stability of enzyme at 0 oC was better than at 4 oC and 25 oC, the enzyme activity decreased until 41,51 % (crude extract), 34,63 % (ammonium sulphate fractionated) and 37,42 % (dialysis) after 12 days incubation.

Abstrak :
ABSTRAK
Daerah Istimewa Yogyakarta merupakan wilayah yang beresiko tinggi terhadap bencana gempabumi mengingat secara tektonik merupakan daerah aktif dengan kegempaan yang tinggi serta tingkat kepadatan penduduk yang relatif tinggi. Data BMKG selama 2008- awal 2015 menunjukkan banyak kejadian gempabumi yang terjadi di Daerah Istimewa Yogyakarta dan sekitarnya, namun banyak gempabumi dangkal memiliki kedalaman yang kurang akurat. Analisis kegempaan membutuhkan data lokasi hiposenter yang akurat. Oleh karena itu relokasi gempabumi diperlukan untuk menunjang analisis kegempaan. Metode Double Difference diterapkan untuk merelokasi data gempabumi. Metode tersebut meminimalkan residual waktu tempuh kalkulasi dan observasi dari sepasang gempabumi berdekatan yang terekam pada stasiun yang sama dengan asumsi raypath kedua gempabumi sama, sehingga kesalahan waktu tempuh akibat model kecepatan yang tidak termodelkan dapat diminimalkan tanpa koreksi stasiun. Hasil dari penelitian untuk zona subduksi menunjukkan pola stress tektonik zona subduksi pada gempabumi dangkal terelokasi dan adanya zona seismik ganda yang menguatkan penelitian terdahulu. Hasil relokasi gempabumi di zona patahan menunjukkan kedalaman Patahan Opak terdangkal mulai dari 3 km hingga terdalam mencapai 17 km. Berdasarkan analisis kegempaan, zona subduksi mengalami aktivitas gempa bumi yang tinggi pada tahun 2014 sampai 2015 dan zona patahan mengalami aktivitas gempabumi yang lebih tinggi di awal periode penelitian dibanding diakhir periode penelitian.

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ABSTRACT
Special Region Yogyakarta has potential seismic hazard for the location is tectonically active with high seismicity and dense population. BMKG data for period 2008 until pre-2015 shows many events occurring in Yogyakarta and surrounding areas, but many shallow earthquakes have depth which is less accurate. Seismic analysis requires accurate hypocenter location data. Therefore relocation is needed to provide seismic analysis. Double Difference method is applied. The method minimizes residuals between calculated and observed travel time of pairs of nearby earthquakes which is recorded on the same station with the assumptions that the raypath is similar, so the travel time errors due to unmodeled velocity structure can be minimized without station correction. The results shows relocated shallow earthquakes followed the tectonic stress trend in subduction zone and double seismic zone which confirmed previous research has appeared. Relocation results in the earthquake fault zone shows the depth of the shallowest Opak Fault ranging from 3 km to the deepest reaches 17 km. Based on the analysis of seismicity, subduction zones experienced high seismic activity in 2014 to 2015 and the fault zone experienced a higher activity at the beginning of the study period compared to the end of the study period.

Abstrak :
Acetonitrile is an organic, derivative of carboxylic acid, and toxic compound. This compound has been widely used in pharmaceutical and chemical industries. Nowadays, there are more interests in acetonitrile-degrading microbes for their potential in chemical syntheses and biological detoxification of nitrile-containing wastes. The aim of this study were to isolate, select, and characterise the isolate from industrial effluents which has the best degrading capability and its acetonitrile-degrading enzyme. Cultures were grown on mineral medium with microelements and acetonitrile was added as sole source of energy, carbon, and nitrogen. Analysis to characterise the acetonitrile-degrading enzyme had been conducted with whole cells of the selected isolate. Decreasing of acetonitrile concentration and formation of its degrading products were determined by gas chromatography and ammonia analysis was done by Nessler's method. Isolate D5, identified as Corynebacterium sp., was able to grow on high concentration acetonitrile (up to 5 % v/v) and exhibited the highest specific growth rate (p) among 29 isolates which could grow on acetonitrile. When Corynebacterium D5 grew on 2 % (vlv) acetonitrile, the doubling time was 6 hours 40 minutes, the specific growth rate (p.) was 0.1 h-1, and the acetonitrile decreasing rate was 3.99 mM/h. Increasing of acetonitrile concentration would extend the doubling time, decline the maximum growth and specific growth rate (M), and biomass production. The products of acetonitrile degradation by Corynebacterium D5 were acetamide, acetic acid, and ammonia. The highest maximum growth of Corynebacterium D5 showed when 13-aminopropionitrile was used as a substrate. Corynebacterium D5 degraded 5 % (v/v) acetonitrile with degrading rate of 0.906 µmol min-' (mg dry weight cells)-'. Corynebacterium D5 hydrolysed acetonitrile by two-step reaction catalysed by nitrile hydratase and amidase. The acetamide forming rate [0.399 pmol min' (mg dry weight cells)-' ] was higher than acetic acid forming rate [0.198 µcool min-' (mg dry weight cells)'' ] and the maximum acetamide concentration formed (about 239 mM) was also higher than maximum acetic acid concentration formed (about 145 mM). Nitrite hydratase activity of Corynebacterium D5 was found to be higher than amidase activity. Maximum nitrite hydratase activity was found out at pH 6 and at 30 °C, while maximum amidase activity was found out at pH 7 and up to 60 °C the activity still increase. Nitrite hydratase of Corynebacterium D5 was totally inhibited by 5 mM Hg2+, whereas amidase was slightly inhibited by 10 mM Co2+.

Abstrak :
Hyaluronidase testicular (E.C.3.2.1.35) adalah enzim yang mendepolimerisasi asam hyaluronat menjadi oligosakarida. Enzim ini digunakan untuk terapi, sebagai spreading factor yang dikombinasikan dengan suatu anastesi lokal. Dalam penelitian ini telah dilakukan pemurnian enzim hyaluronidase dari testis sapi peranakan ongole dengan kromatografi afinitas. Setelah diisolasi menggunakan sukrosa 0,25 M, fraksinasi dengan amonium sulfat, dan dialisis, pemurnian enzim dilakukan menggunakan kromatografi afinitas blue sepharose CL-6B. Dari pemurnian ini diperoleh aktivitas spesifik sebesar 171,45 x 10-3 U/mg dengan tingkat kemurnian 86 kali dan rendemen 39,84% dari ekstrak kasar. Fraksi blue sepharose CL-6B yang diperoleh kemudian dimurnikan dengan kromatografi imunoafinitas CNBr-activated sepharose 4 FF dengan imunoglobulin G spesifik hyaluronidase dan diperoleh aktivitas spesifik sebesar 558,49 x 10-3 U/mg dengan tingkat kemurnian 617 kali dan rendemen 13,50% dari ekstrak kasar. Sedangkan pemurnian hyaluronidase dari fraksi blue sepharose CL-6B yang dilanjutkan dengan kromatografi penukar ion DEAE FF memiliki aktivitas spesifik sebesar 620,80 x 10-3 U/mg dengan tingkat kemurnian 310 kali dan rendemen 37,87% dari ekstrak kasar. Dengan menggunakan elektroforesis gel SDS-PAGE bobot molekul hyaluronidase testis sapi peranakan ongole diperkirakan sebesar 62 kDa. Aktivitas enzim optimum pada pH 5,0 dan fraksi-fraksi hyaluronidase dari tahap pemurnian relatif stabil apabila disimpan pada suhu 0 oC dibanding pada suhu 4 oC dan 25 oC.