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"The kinetics of isothermal phase transformation in tempered embrittlement stainless stell zeron-25 (SAF-2507): The kinetics study of phase transformation in stainless steel SAF 2507 heat-treated at 800,850 and 900 oC have been done.Eitheir observation of microstructure for treated materials by an optical or electron microscope confirmed the formation of carbide phase at grain boundaries between ferrite and austenite lead to three phase materials.It is furthur observed that for the three treated tempereture there were no significant change in volume fraction of territe phase found and thus it may be be assumed constant..Hovewer,this was not the case for two other phase in wich volume fraction of carbide phase show an increase and followed by a decrease in in volume fraction of austenite phase.It is then concluded that the carbide transformed from austenite.The number of volume fraction of carbide phase determinet by XRD methods were ranged from 6.0%to20% depends on time andtemperature of treatments.An avrami equation for kinetic sudy of phase transformation weresuccessively used for construction of phase transformation curves from which some kineticparameters of phase transformation were succesfully derived,among them the avarage constantrate reaction(n) equals to about one,the activation energy below 850oC is 304 and for 850oC above is 307 kj/mol.With kinetics constans above,the complete IT diagram for iso embrittlement of stainless steel SAF 2507 was succesfully built theoretically."

"Pembentukan produk oksidasi kolesterol pada proses pangan maupun kesehatan melibatkan reaksi kimia dan biokimia, reaksi oksidasi kolesterol ini dapat dikontrol melalui model kinetika pada tren oksidasi. Penggunaan model kinetika menjadi salah satu aspek penting dalam memprediksi kadar kolesterol hasil oksidasi. Reaksi oksidasi kolesterol melibatkan enzim sebagai katalisator, yaitu enzim kolesterol oksidase. Bakteri yang digunakan sebagai penghasil enzim kolesterol oksidase yaitu Streptomyces sp. Enzim kolesterol oksidase diproduksi dengan menggunakan metode fermentasi submerged. Untuk meningkatkan efektifitas enzim kolesterol oksidase dalam oksidasi kolesterol, maka dibutuhkan matriks pendukung. Enzim kolesterol oksidase diimobilisasi dengan material magnetit silikon dioksida. Material magnetit silikon dioksida disintesis melalui metode hidrotermal dengan proses pelapisan silika pada partikel magnetit. Reaksi oksidasi dilakukan dengan metode oksidasi secara langsung terhadap substrat. Penelitian ini bertujuan untuk memperoleh enzim kolesterol oksidase dari Streptomyces sp., mengimobilisasi enzim terhadap material magnetit silikon dioksida, estimasi konstanta laju reaksi oksidasi kolesterol, serta membandingkannya dengan enzim bebas dan enzim terimobilisasi. Enzim yang telah diproduksi memiliki aktivitas sebesar 5,12 U/mL. Enzim yang telah diproduksi digunakan untuk imobilisasi dan reaksi oksidasi. Variabel bebas yang digunakan dalam penelitian ini yaitu konsentrasi enzim (5;10;20 mg/mL), konsentrasi substrat (1,64;3,23;6,46 mM) dan bentuk enzim (ekstrak kasar enzim kolesterol oksidase dan enzim kolesterol oksidase terimobilisasi). Hasil karakterisasi FTIR dari material magnetit menunjukkan gugus fungsi M-O di bilangan gelombang 559,88; 598,91 dan 680,1 cm-1 gugus Si-O di bilangan gelombang 1615,78 dan 1761,65 cm-1. Hasil uji oksidasi dengan menggunakan HPLC diperoleh konsentrasi substrat secara optimal dioksidasi oleh enzim terimobilisasi dengan konsentrasi 20 mg/mL serta konsentrasi kolesterol awal 1,94 mM dengan hasil akhir sebesar 0,49 mM, sedangkan enzim kolesterol oksidase bebas mengoksidasi kolesterol dengan hasil akhir sebesar 1,459 mM.

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The formation of products related to reactions and chemical reactions, these reactions can be carried out through the kinetics model on the oxidation trend. The use of kinetics is an important aspect in achieving oxidation cholesterol levels. A catalyst of cholesterol oxidation reaction is a cholesterol oxidase enzyme. The bacteria that used as a producer of cholesterol oxidase enzyme is Streptomyces sp. Cholesterol oxidase enzymes are produced using submerged fermentation methods. To increase the effectiveness of cholesterol enzymes in cholesterol oxidation, a support matrix is needed. The cholesterol oxidase enzyme is immobilized with magnetite silicon dioxide. Magnetite silicon dioxide material is synthesized by using hydrothermal method with silica coating process. The oxidation reaction is carried out by the oxidation method directly against the substrate. The aims of this study are to produce the enzymes from Streptomyces sp., immobilize enzymes to magnetite silicon dioxide, obtaining the rate of oxidation reactions, and comparing data between free enzyme and immobilized enzyme. The produced enzyme activity was 5,12 U/mL, this enzyme is used for immobilization and oxidation reaction. In this study, the independent variables are enzyme concentration (5;10;20 mg/mL), substrate concentration (1,94; 3,23;6,46) and enzyme forms (crude extract cholesterol oxidase enzyme and immobilized enzyme). The FTIR characterization of materials have shown that metal oxide functional groups appeared at wavenumber of 559,88; 598,91 dan 680,1 cm-1- and Si-O groups at wavenumber of 1615,78 dan 1761,65 cm-1. The oxidation test by HPLC showed that the substrate concentration optimizely oxidized by immobilized enzyme with the initial concentration 20 mg/mL and substrate concentration 1,94 mM with final oxidation concentration was 1,94 mM, meanwhile the free enyme with same concentration showed 1,459 mM at final concentration."

"Enzim kolesterol oksidase adalah enzim oksidoreduktase yang mampu mendegradasi kolesterol. Pada percobaan ini, dilakukan produksi enzim kolesterol oksidase oleh Streptomyces sp. melalui fermentasi submerged lalu dilakukan investigasi terhadap aktivitas dan kemampuan katalisis enzim kolesterol oksidase. Pada percobaan, substrat dan enzim divariasikan pada berbagai konsentrasi, yaitu 0,15, 0,075, dan 0,0375 U/mL dan 1,25, 2,5, dan 5 mg/mL. Perbandingan konstanta laju reaksi antara ekstrak kasar enzim dan enzim komersial diperoleh dari hasil penelitian. Perbandingan konstanta laju reaksi enzimatis oleh faktor yang mempengaruhi, diantaranya imobilisasi enzim dan suhu inkubasi enzim, dengan data yang diperoleh dari literatur. Enzim dan substrat mengalami reaksi oksidasi pada waktu inkubasi 5, 30, 65, 120, dan 240, lalu konsentrasi kolesterol residu pada sampel dilakukan plotting dengan waktu inkubasi, dan konstanta laju reaksi diperoleh melalui permodelan reaksi orde 1 dengan pendekatan integrasi numerik Euler. Aktivitas ekstrak kasar enzim yaitu 1,69 U/mL dengan konstanta laju reaksi yaitu 0,01/menit untuk ekstrak kasar enzim dan 0,014/menit untuk enzim komersial. Selanjutnya, diperoleh faktor yang mempengaruhi konstanta laju reaksi oksidasi kolesterol secara enzimatik oleh enzim kolesterol oksidase, yaitu konsentrasi enzim, jenis enzim, imobilisasi, dan suhu inkubasi. Reaksi oksidasi kolesterol oleh enzim kolesterol oksidase dari Streptomyces sp. mengikuti reaksi orde 1.

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Cholesterol oxidase well known as oxidoreductase enzyme which able to degrade the cholesterol. Here, we produced cholesterol oxidase from Streptomyces sp. by submerged fermentation and investigate the activity and cholesterol oxidation kinetics of cholesterol oxidase. The enzyme and substrate are diluted in various concentration, 0.15, 0.075, 0.0375 U mL and 1.25, 2.5, 5 mg mL, respectively. Further step was comparing crude enzyme and commercial enzyme from Streptomyces sp. by oxidation constant rate of reaction. The enzyme and substrate were through the oxidation reaction, and the amount of cholesterol residue in the sample are determined by HPLC. In this work, we also compared the oxidation constant rate of reaction of previous experiment from literature with affecting factors, such as immobilization and incubating temperature. The cholesterol residue in the sample are plotted by time reaction and the rate constant is obtained by first order rate reaction using Euler integration method. The crude enzyme activity is 1.69 U mL and the reaction constant are 0.01 U mL and 0.014 for crude extract and commercial enzyme, respectively. Furthermore, several factors affecting constant rate of enzymatic oxidation of cholesterol were enzyme concentration, enzyme type, immobilization, and incubating temperature. Cholesterol oxidation by Streptomyces sp. cholesterol oxidase was follow the first order reaction."