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"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+."

"Fosfatase asam merupakan enzim yang dapat digunakan untuk teknik ELISA - untuk mengukur kadar suatu zat dalam cairan tubuh yang jumlahnya sangat kecil. Salah satu sumber enzim tersebut adalah air kelapa (Cocos nucifera Linn). Penelitian yang dilakukan oleh Sadavisan (1951), Wilson et al. (1952), Anna Istiqomah (1994) dan Emilia Aisjah (1996) menunjukkan adanya aktivitas enzim fosfatase dalam daging buah dan air kelapa.Penelitian ini adalah mengisolasi dan pemurnian enzim fosfatase asam dari air kelapa. Untuk pemurnian enzim digunakan kromatografi gel dengan Sephadex G-75 dan kromatografi afinitas dengan Gel immobilized p-aminobenzyl phosphonic acid sepharose. Kemurnian enzim diperiksa dengan elektroforesis gel poliakrilamid. Aktivitas enzim secara kuantitatif ditentukan dengan spektrofotometer, dan secara kualitatif dapat dilihat dengan pewarnaan substrat. Kadar protein diukur dengan spektrofotometer pada panjang gelombang 280 nm.Hasil.penelitian ini menunjukkan bahwa dalam air kelapa terdapat enzim fosfatase asam yang ditunjukan oleh satu pita pada elektroforesis gel poliakrilamid.

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Isolation And Purification Of Acid Phosphatase From Coconut Water (Cocos nucifera Linn)Acid phosphatase was detected in coconut. More than fourty years ago, early investigators found this enzyme solely in coconut milk. It is not until recently that the enzyme was also found in coconut water. Recent studies also reported some characteristics of the enzyme from both sources.The purpose of this study is to isolate and to purity acid phosphatase from coconut water. Firstly, the enzyme was precipitated with etanol. After the dialysis in a cellophane bag, the precipitate was redissolved in 0,9% NaCl. The enzyme was separated with Sephadex 0-75, using 0,9% NaCl as eluent. Fractions of 5 mL were collected and each was analysed for the protein contents and for acid phosphatase activities. The fractions of high enzymes activity were pooled and purified, using an affinity chromatography technique with benzoyl phosphonic acid, a competitive inhibition, as a stationary immobilized ligand. Retained enzymes were eluted with 0,2 M NaHHPO4 and fractions of 2 mL were collected.During the study, protein contents were measured with A 280 technique and enzymes activities were assayed with p-nitrophenyl phosphate (p-NPP) as a substrate. In both steps, the purity of the pooled fractions were analysed with a polyacrylamide gel electrophoresis, stained with Coomassie Blue as well as p-NPP-ammonium sulfide, lead acetat for revealing the enzyme.It is found that acid phosphatase could be isolated and purified, as indicated by increasing specific activity and by PAGE analysis, from coconut water, by gel filtration and affinity chromatography technique."

"Ruang Lingkup dan Cara Penelitian: Enzim fosfatase alkali antara lain digunakan dalam teknik ?enzyme immunoassay?, untuk mengukur kadar sesuatu zat dalam cairan tubuh dalam jumlah yang sangat kecil. Dalam penelitian ini diusahakan isolasi dan pemurnian enzim fosfatase alkali dari E. coli. Identifikasi kuman dilakukan dengan agar Endo, agar darah, tes pewarnaan Gram, sifat-sifat biokimia, dan tes serologik. Untuk pemurnian enzim digunakan sonikator, kromatografi pertukaran ion dengan DEAE Biogel, dan kromatografi gel dengan Sephadex G-100. Kemurnian enzim diperiksa dengan elektroforesis pada membran selulosa asetat. Aktivitas enzim secara kuantitatif ditentukan dengan spektrofotometer, dan secara kuaLitatif dapat dilihat dengan agar substrat. Kadar protein diukur dengan metoda Lowry. Terhadap fraksi gel diteliti pengaruh suhu, pH, ion logam, dan jenis bufer atas aktivitas enzim. Demikian pula ditentukan nilai Km dan Vmax, serta reaksi hidrolisis tanpa dan dengan transfosforilasi.Hasil dan Kesimpulan: Kuman diidentifikasi sebagai E. coli non-patogen. Enzim diperoleh setelah fraksi gel dengan ,pemurnian 242 kali dan hasil 59%. Pada eLektroforesis ditemukan kadar protein enzim 52,8%. Enzim memiliki pH optimum 8,0, dan tidak stabil bila diinkubasi selama 1 jam diluar pH optimum. Aktivitas enzimeningkat secara Linier sampai suhu 45° C, dengan koefisien suhu 1,49. Enzim stabil pada inkubasi selama 20 menit pada suhu 25 - 45° C. Aktivitas enzim tidak dipengaruhi penambahan ion Mg dan Zn (0,01 M). Aktivitas meningkat dengan meningkatnya molaritas bufer, Vmax terbesar didapatkan dalam buffer Tris dan Km terkeciL pada bufer AMP. Reaksi hidrolisis dan transfosforilasi berlangsung pada bufer Tris dan AMP, sedangkan pada bufer glisin hanya terjadi reaksi hidrolisis.

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Scope and Method of Study: The enzyme alkaline phosphatase is used among others in enzyme immunoassay, to enable the quantitation of a small amount of substances in body fluids. In this study, an attempt was carried out for the isolation and purification of the enzyme from E. coli. The bacteria was identified through culture on Endo and blood agar, Gram staining, biochemical tests, and serology. The bacteria were disrupted by ultrasonication, and the enzyme purified by ion exchange chromatography on DEAE Biogel followed by gel chromatography on Sephadex G-100. Enzyme purity was examined by electrophoresis on cellulose acetate. Enzyme activity was determined by spectrophotometry, and protein concentration was measured by the method of Lowry. The gel fraction was tested for the effect of pH, temperature, metal ion, and type of buffer. The Km and Vmax was measured, for hydrolysis with and without transphosphorylation.Findings and Conclusions: The bacteria was identified as non-pathogenic E. coli. After gel chromatography the enzyme was purified 242 fold, at 59%, yield. Electrophoresis revealed that the enzyme content was 52.8 %. The enzyme has a pH optimum of 8.0, and it was unstable on standing for 1 hour outside the pH optimum. Enzyme activity increased Linearly with temperature (to 45° C), with a temperature coefficient of 1.49. The enzyme is stable for 20 minutes at 5° - 45++ C, and the activity not influenced by Mg++ and Zn++ ions (0.01 M). The activity increased with increased molarity of the buffer, the highest Vmax was observed with Tris buffer, and the Lowest Km with AMP buffer. Hydrolysis and transphosphorylation occurred in Tris and AMP buffer, while in glycine buffer only hydrolysis was observed."

"Pemuliaan galur Aspergillus melalui cara perbaikan genetik klasik atau molekuler modern biasa dilakukan untuk meningkatkan metabolit sekunder yang dihasilkan. Transformasi genetik kapang sebagian besar bergantung pada persiapan protoplas yang baik, meskipun ada beberapa metode transformasi alternatif yang tidak memerlukan preparasi protoplas. Pada review ini akan dirangkum aplikasi protoplas dan preparasinya dalam metode pemuliaan galur dari berbagai spesies Aspergillus. Beberapa aplikasi dari teknik protoplasting yang telah digunakan untuk melakukan pemuliaan galur pada Aspergillus sp., adalah Protoplast-mediated transformation (PMT), fusi protoplas, UV mutagenesis dengan preparasi protoplas dan Agrobacterium-mediated transformation (AMT). Beberapa sumber enzim potensial juga dibahas pada review ini. PMT adalah metode yang paling umum dan diketahui telah efektif digunakan, namun prosedurnya cenderung rumit dan memiliki tingkat regenerasi yang rendah. Banyak faktor yang berperan dalam peningkatan strain jamur dengan metode protoplasting untuk meningkatkan produk-produk bioteknologi salah satunya adalah pemilihan kombinasi enzim yang optimal untuk melisiskan dinding sel Aspergillus. Crude enzyme dari saluran pencernaan bekicot (Achatina fulica) adalah salah satu alternatif enzim dari alam yang diduga dapat digunakan untuk meningkatkan nilai ekonomis pembentukan protoplas.

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Aspergillus strain improvement through classical or modern molecular genetic improvement is usually done to increase fungal secondary metabolites production. The fungal genetic transformation largely depends on preparation of fungal protoplasts, although there are several alternative transformation methods that do not require protoplast preparation. This review will summarize the application of protoplast and its preparation in the strain improvement method of various Aspergillus species. Some applications of the protoplast isolation which have been used in strain improvement of Aspergillus sp. are Protoplast-mediated transformation (PMT), protoplast fusion, UV mutagenesis with protoplast preparation and Agrobacterium-mediated transformation (AMT). Several potential enzyme sources are also discussed in this review. PMT is the most common method and known that it has been effectively used, but the procedure tends to be complicated and have a low regeneration rate. Many factors play a role in improving fungal strains to increase biotechnological products by the protoplast isolation, one of which is the selection of an optimal enzyme combination to lyse the Aspergillus cell wall. Crude enzyme from gut juice of African Giant snail (Achatina fulica) is an alternative nature enzyme that could be able to be used to increase the economics value of protoplast formation."

"Helicobacter pylori has been known as a cause of chronic gastritis, a predisposition to gastric and duocenal ulcers, and a class I gastric carcinogen. Throughout the world, H. pylori infection is very common, reaching 40% -50% of the population in developed nations and 80% - 90% of the population in developing nations.

Several techniques have been used to detect H. pylori infection, such as the urea breath test, rapid urease test, serological test, as well as biopsies of gastric or duodenal tissues for culture and histopathology. In this review article, we will discuss a relatively new method to detect H. pylori antigen in stools with enzyme immunoassay, and comparisons with other standard techniques. However, the H. pylori stool antigen test is not yet commercially available in Indonesia.

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"Untuk pengobatan dan pencegahan pada wanita menopause akibat kekurangan hormon estrogen adalah dengan pemberian hormon estrogen yang dikenal dengan istilah hormone replacement therapy (HRT). Cara pemberian HRT yang banyak digunakan adalah berupa tablet. Pemberian tablet akan terjadi metabolisme di usus dan hati. Tablet harus digunakan setiap hari sehingga menimbulkan kebosanan dan menimbulkan gangguan gastrointestinal. Pemberian berupa jel cukup dioles di badan dan tidak terjadi metabolisme di usus dan hati. Pada wanita dengan uterus, estrogen harus dikombinasikan dengan progestogen. Jenis progestogen yang dianjurkan adalah jenis turunan alamiah dan yang memiliki sifat antimineralokortikoid, sehingga tidak menyebabkan retensi cairan. Salah satu jenis progestogen yang tidak menyebabkan retensi cairan adalah nomogestrol acetate. Nomogestrol acetate juga menghambat enzim 17β Hidroksisteroiddehydrogense tipe 1 sehingga estradiol (E2) tidak dapat diubah menjadi estron (E1). Akibatnya kadar E2 di dalam jaringan payudara rendah dan dengan sendirinya menurunkan risiko kanker payudara. (Med J Indones 2003; 12: 194-8)

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The treatment and prevention of disease in menopausal women due to deficiency of estrogen hormone are done through the administration of estrogen hormone, known as hormone replacement therapy (HRT). The administration of HRT is commonly done through the administration of tablets. However, the administration of tablet will result in metabolism in the colon and liver. Tablets are usually used on a daily basis such that it may lead to boredom and results in gastrointestinal disorder. The administration of gel, on the other hand, is done by applying the gel to the body and therefore metabolism in the colon and liver can be prevented. In women with uterus, estrogen must be combined with progestogen. The type of progestogen recommended is the one with natural derivative and which possesses antimineralocorticoid properties, such that fluid retention can be avoided. One of the types of progestogen which does not result in fluid retention is nomogestrol acetate. Nomogestrol acetate will also inhibit 17β hydrosisteroiddehydrogency enzyme type 1, such that estradiol (E2) is prevented from being transformed into estron (E1). As a result, E2 level in the breast tissue is kept at minimum, thereby reducing the risk of breast cancer. (Med J Indones 2003; 12: 194-8)"

"One of the alternative media , which is potential to be developed is the use of natural fiber materials from the environment (indigenous material)....."