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Caroline Christina
Produksi Kolagen dari Membran Cangkang Telur Ayam dan Analisis Kandungan Hidroksiprolin Menggunakan Kromatografi Cair Kinerja Tinggi Detektor Fluoresensi = Collagen Production From Chicken's Eggshell Membrane and Analysis of its Hydroxyproline Content Using High Performance Liquid Chromatography-Fluorescence Detector
"ABSTRAK
Telur merupakan salah satu makanan yang dinikmati oleh seluruh kalangan di dunia. Hal ini menyebabkan cangkang telur menjadi salah satu limbah terbesar yang disebabkan oleh unggas. Limbah dapat mengotori lingkungan padahal cangkang telur ayam yang salah satu penyusunnya membran cangkang telur, memiliki manfaat sebagai sumber kolagen. Membran cangkang telur merupakan bagian yang berada tepat pada lapisan dalam telur. Ekstraksi perlu dilakukan untuk mendapatkan kolagen dari membran cangkang telur ayam. Hidroksiprolin merupakan salah satu asam amino sekunder yang merupakan penanda adanya kolagen yang perlu diderivatisasi menggunakan FMOC-Cl (9-Fluorenilmetoksikarbonil-klorida) untuk dianalisis dengan KCKT. Penelitian ini bertujuan untuk memperoleh metode optimal dalam ekstraksi kolagen dalam membran cangkang telur ayam dan analisis penentuan kadar kolagen hasil metode optimal menggunakan KCKT-detektor fluoresensi. Ekstraksi kolagen dari membran cangkang telur ayam perlu dioptimalisasi untuk menghasilkan jumlah yang optimal. Optimalisasi ekstraksi pada penelitian ini dilakukan dengan tiga parameter yaitu, metode (hidrolisis asam, hidrolisis enzim, dan campuran keduanya), suhu (4oC dan 22-23oC), dan ada atau tidak adanya pengadukan. Berdasarkan penelitian ini, didapatkan metode paling optimal adalah pada ekstraksi dengan hidrolisis asam pada suhu 4oC tanpa pengadukan yang menghasilkan rendemen 0,608% dengan kadar kolagen 2,4666% dari total hasil ekstraksi.
ABSTRACT
Chicken eggs are one of the food that most enjoyed by all people in the world. The consumption of eggs cause eggshell to be one of the biggest waste. However, the eggshell has its own benefits. The eggshell membrane, located right in the inner layer of the egg, contains collagen. Extraction needs to be done to obtain collagen from the chicken eggshell membrane. Hydroxyproline, a secondary amino acid, is a marker of collagen that needs to be derivatized using FMOC-Cl (9-Fluorenylmethoxycarbonyl-chloride) so, it could be analyzed with HPLC. This study aims to obtain an optimal method for collagen extraction from chicken eggshell membranes and its optimal method collagen content analysis using HPLC-fluorescence detector. Collagen extraction from the chicken eggshell membrane needs to be optimized to produce an optimal amount. Extraction optimization in this study was carried out with three parameters, which were, method (acid hydrolysis, enzyme hydrolysis, and mixture of both), temperature (4oC and 22-23oC), and the presence or absence of stirring. Based on this research, the most optimal method was extraction with acid hydrolysis at 4oC without stirring which results in 0,608% yield with collagen content of 2,4666%.
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Depok: Fakultas Farmasi Universitas Indonesia, 2020
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UI - Skripsi Membership  Universitas Indonesia Library
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Savira Ayusandra Putri
Produksi Kolagen dari Limbah Membran Cangkang Telur Bebek dan Analisis Kandungan Hidroksiprolin Secara Kromatografi Cair Kinerja Tinggi-Fluoresensi = Collagen Production from Duck Eggshell Membrane Waste and Analysis of Hydroxyproline Content by High Performance Liquid Chromatography–Fluorescence
"Dalam jangka waktu satu tahun, Indonesia dapat menghasilkan 33.000 hingga 39.000 ton limbah cangkang telur bebek. Jumlah limbah cangkang telur bebek yang besar memiliki potensi untuk diolah menjadi sesuatu yang bernilai ekonomis dan menciptakan nilai baru dengan memanfaatkan membrannya untuk produksi kolagen. Penelitian ini bertujuan untuk memperoleh metode ekstraksi yang optimum dengan menggunakan dua faktor utama sebagai variasi kondisi perlakuan dan memperoleh kadar kolagen dengan menganalisis senyawa hidroksiprolin pada membran cangkang telur bebek. Variasi tersebut yaitu suhu (4°C dan 22-23°C) dan kondisi dengan adanya pengadukan dan tanpa adanya pengadukan. Pada proses pre-treatment, membran direndam menggunakan NaOH 0,1 M dan ekstraksi dilakukan dengan tiga cara yaitu ekstraksi menggunakan larutan asam asetat 0,5 M, menggunakan larutan enzim pankreatin 4NF 0,1%, dan menggunakan larutan keduanya. Tahap selanjutnya untuk mendapatkan kolagen padat dilakukan proses freeze drying. Sampel kolagen padat kemudian diderivatisasi menggunakan FMOC-CI (9-Fluorenilmetoksikarbonil klorida). Sampel dianalisis dengan kromatografi cair kinerja tinggi menggunakan kolom C18 dan detektor fluoresensi pada panjang gelombang eksitasi 255 nm dan emisi 320 nm. Fase gerak yang digunakan untuk analisis adalah larutan dapar asetat (pH 4,2) – asetonitril (60:40) dengan laju alir 0,8 mL/menit. Hasil penelitian menunjukkan ekstraksi dengan larutan asam asetat 0,5 M pada suhu 4°C tanpa adanya pengadukan merupakan metode yang optimum, sehingga diperoleh rendemen kolagen sebesar 1,284% dan kadar rata-rata kolagen 1,9488%.
Within the span of a year, Indonesia has the capability to produce 33,000 to 39,000 tons of duck eggshell waste. A large amount of duck eggshell waste has the potential to be processed into something of economic value as well as generating new value by utilizing the membrane for collagen production. The aimed of this study was to obtain the optimum extraction method by the use of two main factors as variations in the treatment conditions and quantified collagen content by analyzed hydroxyproline in duck eggshell membrane. These variations include temperatures (4°C and 22-23°C) along with conditions, namely, with and without stirring. During the pre-treatment processed, the membranes were soaked using 0.1 M NaOH, and the extraction was carried out in three ways, by using 0.5 M acetic acid solution, 0.1% NF pancreatic enzyme solution, and both solutions. The next step in the formation of solid collagen was the freeze drying process. Solid collagen samples were then derivatized by using FMOC-CI (9-Fluorenylmethoxycarbonyl chloride). The samples were analyzed by high performance liquid chromatography used column C18 and fluorescence detector at excitation wavelength of 255 nm and emission wavelength of 320 nm. The mobile phase used for the analysis was acetate buffer (pH 4.2) - acetonitrile (60:40) with a flow rate of 0.8 mL/min. The results showed that extraction with 0.5 M acetic acid solution at 4°C without the presence of stirring was the optimum method. The collagen yield was 1.284% with average collagen content was 1.9488%."
Depok: Fakultas Farmasi Universitas Indonesia, 2020
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UI - Skripsi Membership  Universitas Indonesia Library
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Ayu Aditya Andayani
Isolasi, pemurnian, dan karakterisasi kolagen dari kulit babi serta analisis kandungan glisin, prolin, dan hidroksiprolin secara kromatografi cair kinerja tinggi-fluoresensi = Isolatio, purification, and characterization of porcine skin collagen and analysis component of glycine, proline, and hydroxyproline by high performance liquid chromatography-fluorescence
"Kolagen merupakan bahan baku tinggi protein, dimana hampir semua asam amino terkandung didalamnya dengan kandungan terbesarnya adalah glisin, prolin, dan hidroksiprolin. Pada penelitian ini, kolagen diisolasi, dimurnikan, dan dikarakterisasi dari kulit babi Sus scrofa domesticus. kemudian dilakukan pencarian kondisi analisis optimum untuk mendapatkan metode penetapan kadar asam amino glisin, prolin, dan hidroksiprolin pada sampel kolagen kulit babi. Metode terbaik untuk mengisolasi kolagen dari kulit babi menggunakan perendaman dalam NaOH 0,1. dan diekstraksi dengan asam asetat 0,5 N, dipresipitasi dengan NaCl 0,9M kemudian disentrifugasi, dialisis sebagai proses pemurnian, dan terakhir di freeze-drying untuk memperoleh bentuk padatnya.
Karakterisasi yang dilakukan meliputi uji organoleptis, pH, analisis gugus fungsi, kadar air, kadar abu, viskositas, dan pewarnaan Casson's trichrome pada jaringan kolagen. Selanjutnya kolagen dihidrolisis dengan HCl 6N selama 24 jam lalu diderivatisasi menggunakan pereaksi 9-Fluorenilmetoksikarbonil klorida FMOC-Cl. Sampel selanjutnya dianalisis menggunakan kromatografi cair kinerja tinggi KCKT dengan kolom C-18 dan detektor fluoresensi pada panjang gelombang eksitasi 265 nm dan panjang gelombang emisi 320 nm. Fase gerak yang digunakan dapar asetat pH 4,2 -asetonitril 55:45 dengan laju alir 0,8 mL/menit. Hasil menunjukkan kadar rata-rata glisin, prolin, hidroksiprolin berturut-turut adalah 33,663 0,215. 12,333 0,128. dan 11,303 0,354.
Collagen is. high protein feedstock with almost all amino acids are contained in it, but the greatest content of all are glycine, proline, and hydroxyproline. In this study, collagen was isolated, purified, and characterized from porcine skin Sus scrofa domesticus. then determination of the optimum conditions analysis on amino acid in collagen were performed to obtain. method for determination of glycine, proline, and hydroxyproline content in porcine skin collagen samples. The best method to isolate collagen was using 0.1. NaOH, extracted with 0.5. Qacetic acid, precipitated with 0.9M NaCl, then collagen was centrifuged, dialysed to purification, and freeze dryed to get the solid form.
The characterization tests includes organoleptic, pH, Fourier Transform Infra Red analysis, moisture content, ash content, viscosity, and Casson 39. trichrome staining on collagen tissue. After that, collagen was hydrolized using HCl 6N for 24 hours then derivatized using. Fluorenylmethylcarbonyl chloride. Collagen was analyzed using high performance liquid chromatography HPLC with. 18 column and fluorescence detector at excitation wavelength of 265 nm and emission wavelength of 320 nm. Mobile phase used was acetic buffer pH 4.2 acetonitrile 55 45 with flow rate 0.8 mL min. The results showed average contents of glycine, proline, and hydroxyproline were 33,663 0,215 12,333 0,128 and 11,303 0,354."
Depok: Fakultas Farmasi Universitas Indonesia, 2017
S68082
UI - Skripsi Membership  Universitas Indonesia Library
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Dwi Yulianti
Isolasi, pemurnian, dan karakterisasi kolagen dari tendon sapi serta analisis kandungan glisin, prolin, dan hidroksiprolin secara kromatografi cair kinerja tinggi-fluoresensi = Isolation purification and characterization of bovine tendon collagen and analysis of glycine, proline, and hydroxyproline by high performance liquid chromatography-fluorescence
"Kolagen merupakan jenis protein fungsional yang tersusun dalam bentuk triple helix, kandungan asam amino yang paling banyak dalam kolagen yaitu glisin, prolin, dan hidroksiprolin. Pada penelitian ini bertujuan untuk mengisolasi, memurnikan, dan mengetahui karakteristik kolagen hasil isolasi dari tendon sapi serta pencarian kondisi analisis optimum untuk memperoleh kadar glisin, prolin, dan hidroksiprolin. Metode isolasi kolagen yang dilakukan adalah menggunakan NaOH 0,1. sebagai langkah pre-treatment, asam asetat 0,5. untuk proses ekstraksi, salting out dengan NaCl 0,9 M, kemudian dilakukan sentrifugasi dan proses dialisis sebagai proses pemurnian, lalu freeze drying untuk mendapatkan hasil kolagen padat.
Karakterisasi kolagen yang dilakukan yaitu uji organoleptis, pH, kadar air, kadar abu, viskositas, gugus fungsi, dan pewarnaan Casson's trichrome. Selanjutnya kolagen dihidrolisis dengan HCl. N selama 24 jam, serta dilakukan proses derivatisasi menggunakan pereaksi 9-Fluorenimetoksikarbonil klorida FMOC-Cl. Kemudian kolagen dianalisis dengan kromatografi cair kinerja tinggi dengan kolom C18 dan detektor fluoresensi pada panjang gelombang eksitasi 265 nm, dan emisi 320 nm. Fase gerak yang digunakan adalah dapar asetat pH 4,2 ndash; Asetonitril 55:45 dengan laju alir 0,8 mL/menit. Berdasarkan hasil yang didapat menunjukkan kadar rata-rata glisin 33,247 0,20. prolin 11,867 0,20. dan hidroksiprolin 10,51 0,23.
Collagen is. type of functional protein that is composed of the triple helix form, the most abundant amino acids in collagen are glycine, proline, and hydroxyproline. In this study, collagen was isolated, purified, and characterized from bovine tendon, then determined of the optimum condition analysis to obtain glycine, proline, and hydroxyproline. Collagen isolation process used NaOH 0.1. as. pretreatment, acetic acid 0.5. as extraction process, salting out process with NaCl 0.9 M, centrifugation and dialysis process to purification. and then freeze drying as the final stage.
The characterization test of collagen include organoleptic, pH, moisture content, viscosity, ash content, FTIR analysis, and staining Casson 39. trichrome. Then, collagen was hydrolyzed using HCL. N for 24 hours, and derivatized using. Fluorenymethoxycarbonil chloride FMOC Cl. After that, collagen was analyzed using high performance liquid chromatography HPLC with. 18 column and fluorescence detector at excitation wavelength of 265 nm, emission wavelength of 320 nm. Mobile phase used acetic buffer pH 4.2 ndash Acetonitrile 55 45 with flow rate 0.8 mL minute. The results showed average contents of glycine 11.867 0.20. proline 33.247 0.20. and hydroxyproline 10.51 0.23 "
Depok: Fakultas Farmasi Universitas Indonesia, 2017
S68068
UI - Skripsi Membership  Universitas Indonesia Library
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Milza Lubnan
Validasi metode analisis hidroksiprolin dalam kolagen UC-II secara kromatografi cair kinerja tinggi (KCKT)-fluoresensi = Validation methods analysis hydroxyproline from collagen UC-II with high performance liquid chromatography-fluoresence
"ABSTRAK
Undenatured Collagen merupakan kolagen tidak terdenaturasi tipe II yang berasal dari tulang rawan sternum ayam. UC II mengandung beberapa asam amino, salah satunya yaitu hidroksiprolin. Hidroksiprolin merupakan salah satu asam amino sekunder yang merupakan turunan dari prolin yang terdapat pada kolagen. Penelitian ini bertujuan untuk memperoleh metode yang valid pada sediaan UC-II dengan menggunakan kromatografi cair kinerja tinggi dengan detektor fluoresensi. Senyawa hidroksiprolin merupakan senyawa yang tidak memiliki gugus kromofor sehingga perlu dilakukan derivatisasi menggunakan FMOC-Cl 9-Fluorenilmetoksikarbonil- klorida. Berdasarkan kondisi analisis optimum yang didapat senyawa dideteksi pada panjang gelombang eksitasi 255 nm dan emisi pada panjang gelombang 320 nm. Fase gerak yang optimum digunakan untuk analisis adalah larutan dapar asetat pH 4,2 -asetonitril 60:40 dengan laju alir 1,0 mL/menit. Metode yang diperoleh valid dengan linearitas y = 3249704x 141945072; nilai r=0,9994 pada rentang 4-15 ppm. Hasil LOD yaitu 0,49 dan LOQ 1,64. Hasil menunjukkan kadar rata-rata hidroksiprolin adalah 98,66, 99,12, dan 99,85.
ABSTRACT
Undenatured Collagen UC II is a non denatured collagen type II which derived from chicken sternum cartilage. UC II contains several amino acids, one of which is hydroxyproline. Hydroxyproline is one of the secondary amino acids that is derived from the proline contained in collagen. Hydroxyproline is a compound that does not have chromophore group so it has to be derivatived first using FMOC Cl 9 Fluorenylmetoxycarbonyl chloride. This study aimed to obtain a valid method on UC II preparations using high performance liquid chromatography with fluorescence detector. The optimal wavelength for hydroxyproline analysis was 255 nm for excitation and 320 for emission. The optimum mobile phase used for the analysis was buffer acetate pH 4,2 acetonitrile 60 40 with a flow rate 1.0 mL min. The obtained method was valid with linearity y 3249704x 141945072 value r 0.9994 in the range of 4 15 ppm. The result of LOD is 0,49 and LOQ 1,64. The results showed the average level of hydroxyproline were 98,66, 99,12, and 99,85. "
2018
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UI - Skripsi Membership  Universitas Indonesia Library
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Rezta Fadhilah Ramadhanty
Optimalisasi Proses Pengeringan pada Produksi Kolagen dari Membran Cangkang Telur Ayam = Optimization of Drying Process of Collagen Production from Chicken Eggshell Membrane
"Kolagen merupakan protein yang berbentuk triple helix. Kolagen pada membran cangkang telur memiliki stabilitas suhu yang cukup rendah, yaitu sekitar 55oC, sehingga dalam pengeringannya lebih umum digunakan metode liofilisasi. Pada penelitian ini, dilakukan optimalisasi proses pengeringan kolagen dengan metode pengeringan lain yaitu dengan menggunakan oven vakum skala laboratorium dengan tujuan untuk mengurangi biaya produksi. Ekstraksi kolagen dari membran cangkang telur ayam dilakukan dengan menggunakan NaOH 0,1 N pada tahap pre-treatment dan asam asetat 0,5 M pada tahap ekstraksi. Ekstrak kolagen akan melalui tahap pemisahan dengan sentrifugasi, pengendapan dengan NaCl; dan dimurnikan dengan membran dialisis. Ekstrak kolagen dikeringkan dengan oven vakum pada suhu 45oC; 40oC; dan 35oC. Parameter yang digunakan untuk menentukan proses pengeringan yang optimal adalah waktu pengeringan, laju pengeringan, dan kadar total kolagen. Suhu 45oC memberikan hasil waktu pengeringan paling cepat, yaitu 11-12 jam. Kadar kolagen dianalisis dengan Kromatografi Cair Kinerja Tinggi menggunakan kolom Purospher® C18 dan detektor fluoresensi. Kondisi analisis dilakukan pada panjang gelombang eksitasi 255 nm dan emisi 320 nm. Komposisi fase gerak dapar asetat (pH 4,2) dan asetonitril (60:40) dengan laju alir 0,8 ml/menit. Kadar rata-rata total kolagen yang diperoleh pada sampel dengan suhu pengeringan 45oC; 40oC; dan 35oC adalah 2,3517%; 2,2427%; dan 1,9209%.
Collagen is a triple helix shaped protein. Collagen from chicken eggshell membrane has a low thermal stability compared to other collagen source, around 55oC, hence the drying method to obtain collagen is usually by lyophilization. In this study, collagen is dried using vacuum oven laboratory scale to reduce the production cost. Extraction of collagen from chicken eggshell membrane is done using NaOH 0.1 N in pretreatment stage and acetate acid 0.5 M for extraction. Collagen extract is then centrifugated to separate the collagen molecule, precipitated using NaCl, and purificated using the dialysis membrane. Collagen extract dried using vacuum oven at three different temperature, 45oC; 40oC; and 35oC. Optimalization of the drying process is analyzed by observing the drying time, drying rate, and total collagen content obtained. The shortest drying time is 11-12 hours on 45oC. Collagen analyzed using High Pressure Liquid Chromatography with fluoresence detector using Purospher® C18 column, exitation and emission wavelength at 255 nm and 320 nm, mobile phase composition of acetate buffer (pH 4.2) and acetonitrile (60:40), and flow rate 0.8 ml/min. Average total collagen content obtained from sample of drying temperature of 45oC; 40oC; and 35oC are 2.3517%; 2.2427%; and 1.9209%."
Depok: Fakultas Farmasi Universitas Indonesia, 2020
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UI - Skripsi Membership  Universitas Indonesia Library
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Siti Julia
Karakterisasi material organik dari lapisan dalam rempela ayam = Characterization of organic material from chicken gizzards lining
"[Penelusuran kolagen dari lapisan dalam rempela ayam kampung dan ayam negri diidentifikasi dengan cara tanpa perendaman dan dengan perendaman basa NaOH. Sifat fisiokimia kolagen dikarakterisasi dengan menggunakan Fourier Transform Infra Red (FTIR), Scanning Electron Microscopy (SEM), Energy Dispersive X-Ray (EDX) dan Sodium Dodecyl Sulphate – Polyacrylamide Gel Electrophoresis (SDS PAGE). Keberadaan kolagen dari sampel tanpa perendaman diketahui dari gugus fungsi molekul khas yang menyerap radiasi infra merah pada bilangan gelombang tertentu. Pada sampel dengan perendaman basa NaOH, memperlihatkan hilangnya gugus amida pada beberapa daerah jangkauan bilangan gelombang. Selain itu, perendaman juga mengurangi semua komponen kolagen dalam sampel. Kolagen yang berasal dari lapisan dalam rempela ayam merupakan kolagen tipe I dari hasil pemeriksaan bobot unit molekul sampel dengan uji SDS PAGE. Bentuk morfologi dari kolagen ini adalah berbentuk serat kecil dengan partikel-partikel kecil yang teramati menutup serat pada perbesaran kecil. Sementara kandungan atom penyusunnya merupakan susunan umum atom yang terdapat pada protein yaitu karbon, oksigen, fosfor dan sulfur dengan sedikit unsur pengotor.
The collagen resulted from inner layer of free-range chicken and broiler chicken gizzard were identified by means of submersion with NaOH base and without submersion. The physiochemical of collagen were characterized with Fourier Transform Infra Red (FTIR), Scanning Electron Microscopy (SEM), Energy Dispersive X-Ray (EDX) andSodium Dodecyl Sulphate – Polyacrylamide Gel Electrophoresis (SDS PAGE). The presence of collagens in sample without submersion were observed from typical molecular functional group absorbing infrared radiation at a particular wave number. Futhermore, in the sample with NaOH base submersion demonstrated that the loss of amide groups in some range areas of wave number. In addition, the submersion bring about decreating all component of collagen in sample as well. The collagens derived from inner layer of gizzard chicken were type I of collagen resulted from examination the sample unit weight with SDS PAGE. The morphology of collagens were a small fibers with small particles covered fibers in small magnification. The content of the contituent atoms were general arrangement of atoms in the protein such as oxygen, phospor and sulphur with slight impurities.;The collagen resulted from inner layer of free-range chicken and broiler chicken gizzard were identified by means of submersion with NaOH base and without submersion. The physiochemical of collagen were characterized with Fourier Transform Infra Red (FTIR), Scanning Electron Microscopy (SEM), Energy Dispersive X-Ray (EDX) andSodium Dodecyl Sulphate – Polyacrylamide Gel Electrophoresis (SDS PAGE). The presence of collagens in sample without submersion were observed from typical molecular functional group absorbing infrared radiation at a particular wave number. Futhermore, in the sample with NaOH base submersion demonstrated that the loss of amide groups in some range areas of wave number. In addition, the submersion bring about decreating all component of collagen in sample as well. The collagens derived from inner layer of gizzard chicken were type I of collagen resulted from examination the sample unit weight with SDS PAGE. The morphology of collagens were a small fibers with small particles covered fibers in small magnification. The content of the contituent atoms were general arrangement of atoms in the protein such as oxygen, phospor and sulphur with slight impurities.;The collagen resulted from inner layer of free-range chicken and broiler chicken gizzard were identified by means of submersion with NaOH base and without submersion. The physiochemical of collagen were characterized with Fourier Transform Infra Red (FTIR), Scanning Electron Microscopy (SEM), Energy Dispersive X-Ray (EDX) andSodium Dodecyl Sulphate – Polyacrylamide Gel Electrophoresis (SDS PAGE). The presence of collagens in sample without submersion were observed from typical molecular functional group absorbing infrared radiation at a particular wave number. Futhermore, in the sample with NaOH base submersion demonstrated that the loss of amide groups in some range areas of wave number. In addition, the submersion bring about decreating all component of collagen in sample as well. The collagens derived from inner layer of gizzard chicken were type I of collagen resulted from examination the sample unit weight with SDS PAGE. The morphology of collagens were a small fibers with small particles covered fibers in small magnification. The content of the contituent atoms were general arrangement of atoms in the protein such as oxygen, phospor and sulphur with slight impurities.;The collagen resulted from inner layer of free-range chicken and broiler chicken gizzard were identified by means of submersion with NaOH base and without submersion. The physiochemical of collagen were characterized with Fourier Transform Infra Red (FTIR), Scanning Electron Microscopy (SEM), Energy Dispersive X-Ray (EDX) andSodium Dodecyl Sulphate – Polyacrylamide Gel Electrophoresis (SDS PAGE). The presence of collagens in sample without submersion were observed from typical molecular functional group absorbing infrared radiation at a particular wave number. Futhermore, in the sample with NaOH base submersion demonstrated that the loss of amide groups in some range areas of wave number. In addition, the submersion bring about decreating all component of collagen in sample as well. The collagens derived from inner layer of gizzard chicken were type I of collagen resulted from examination the sample unit weight with SDS PAGE. The morphology of collagens were a small fibers with small particles covered fibers in small magnification. The content of the contituent atoms were general arrangement of atoms in the protein such as oxygen, phospor and sulphur with slight impurities., The collagen resulted from inner layer of free-range chicken and broiler chicken gizzard were identified by means of submersion with NaOH base and without submersion. The physiochemical of collagen were characterized with Fourier Transform Infra Red (FTIR), Scanning Electron Microscopy (SEM), Energy Dispersive X-Ray (EDX) andSodium Dodecyl Sulphate – Polyacrylamide Gel Electrophoresis (SDS PAGE). The presence of collagens in sample without submersion were observed from typical molecular functional group absorbing infrared radiation at a particular wave number. Futhermore, in the sample with NaOH base submersion demonstrated that the loss of amide groups in some range areas of wave number. In addition, the submersion bring about decreating all component of collagen in sample as well. The collagens derived from inner layer of gizzard chicken were type I of collagen resulted from examination the sample unit weight with SDS PAGE. The morphology of collagens were a small fibers with small particles covered fibers in small magnification. The content of the contituent atoms were general arrangement of atoms in the protein such as oxygen, phospor and sulphur with slight impurities.]"
Depok: Fakultas Matematika dan Ilmu Pengetahuan Alam Universitas Indonesia, 2014
S57906
UI - Skripsi Membership  Universitas Indonesia Library
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Annisa Ul Latifah
Fabrikasi Perancah berbasis Kolagen dari Ekstrak King Kobia/Alginat/PVA = Fabrication of Collagen-based Scaffolds from King Kobia Extract/Alginate/PVA
"Tulang adalah jaringan ikat dan merupakan bagian tubuh paling penting. Cacat tulang akibat trauma dan penyakit tulang menjadi salah satu masalah yang signifikan saat ini. Osteoarthritis (OA) adalah salah satu penyakit tulang rawan dengan prevalensi yang terus meningkat setiap tahunnya. Rekayasa jaringan tulang menjadi pengobatan alternatif dengan kombinasi sel, perancah, dan faktor sinyal. Perancah tulang harus memiliki sifat mekanik yang serupa dengan tulang, biokompatibilitas, dan biodegradabilitas yang baik. Pemilihan material yang tepat sangat penting dalam pembuatan perancah tulang karena biomaterial memiliki peranan penting dalam rekayasa jaringan tulang. Biomaterial seperti logam, polimer natural, polimer sintetis, keramik, dan kompositnya telah banyak digunakan dalam aplikasi biomedis. Kolagen tipe I merupakan salah satu biomaterial yang sering digunakan untuk perancah tulang. Pada penelitian ini, kolagen diekstrak dari ikan king kobia menggunakan metode deep eutectic solvent (DES). Kolagen tipe I hasil ekstraksi dengan metode DES memiliki yield sebesar 20.318%. Kolagen dikarakterisasi menggunakan SEM dan FTIR. Kolagen hasil ekstraksi digunakan dapat digunakan sebagai material perancah tulang dengan campuran alginat dan PVA. Perancah Kol/Alg/PVA dikarakterisasi dengan pengujian SEM, FTIR, uji tekan, porositas, laju degradasi, dan swelling. Perancah Kol/Alg/PVA memiliki porositas sebesar 29,98% dan memiliki laju degradasi yang bagus. Hasil karakterisasi menunjukkan bahwa perancah dapat digunakan untuk aplikasi perancah tulang.
Bones are connective tissue and are the most important part of the body. Bone deformities due to trauma and bone disease are a significant problem today. Osteoarthritis (OA) is a cartilage disease with a prevalence that continues to increase every year. Bone tissue engineering is an alternative treatment with a combination of cells, scaffolds and signaling factors. Bone scaffolds must have mechanical properties similar to bone, good biocompatibility and biodegradability. Selection of the right material is very important in the manufacture of bone scaffolds because biomaterials play an important role in bone tissue engineering. Biomaterials such as metals, natural polymers, synthetic polymers, ceramics and their composites have been widely used in biomedical applications. Type I collagen is one of the most frequently used biomaterials for bone scaffolding. In this study, collagen was extracted from king kobia fish using the deep eutectic solvent (DES) method. Type I collagen extracted using the DES method has a yield of 20.318%. Collagen was characterized using SEM and FTIR. Extracted collagen can be used as a bone scaffolding material with a mixture of alginate and PVA. Col/Alg/PVA scaffolds were characterized by SEM, FTIR, compression test, porosity, degradation rate, and swelling. The Col/Alg/PVA scaffold had a porosity of 29.98% and had a good degradation rate. The characterization results show that the scaffold can be used for bone scaffold applications."
Depok: Fakultas Teknik Universitas Indonesia, 2023
S-pdf
UI - Skripsi Membership  Universitas Indonesia Library
cover
Erna Pujiningtyas
Formulasi serum yang mengandung fitosom ekstrak biji lengkeng (dimocarpus longan lour) menggunakan koproses kasein kolagen sebagai eksipien = Serum formulation containing longan seed extract (dimocarpus longan lour) phytosome using a coprocess of casein collagen as an excipient/ Erna Pujiningtyas
"ABSTRAK
Biji lengkeng (Dimocarpus longan Lour.) memiliki kandungan polifenol yang memiliki aktivitas antioksidan dan efek penghambatan tirosinase. Fitosom adalah nanovesikel lipid yaitu suatu sistem pembawa obat terutama ekstrak tumbuhan yang dapat meningkatkan absorpsi obat. Tujuan penelitian ini untuk memformulasi sediaan serum yang mengandung fitosom ekstrak biji lengkeng menggunakan koproses kasein-kolagen sebagai eksipien. Digunakan koproses kasein dengan kolagen karena kolagen memiliki manfaat dalam menjaga elastisitas kulit. Metode peredaman DPPH (2,2-Difenil-1-pikril hidrazil) digunakan untuk mengetahui nilai efficient concentration (EC50) ekstrak biji lengkeng dan uji penghambatan tirosinase dilakukan berdasarkan pengukuran dopakrom untuk memperoleh nilai inhibition concentaration (IC50). Efisiensi penjerapan fitosom dihitung berdasarkan penetapan kadar fenol total supernatan dengan metode Folin-Ciocalteu. Nilai EC50 dari ekstrak biji lengkeng sebesar 6,58 μg/mL. Uji penghambatan aktivitas tirosinase menunjukkan nilai IC50 sebesar 1795,93 μg/mL. Pembuatan fitosom dengan perbandingan fosfatidilkolin dan ekstrak sebesar 1,5 : 1 menunjukkan nilai efisiensi penjerapan sebesar 65,88%, nilai rata-rata diameter partikel (Z-average) sebesar 382,59 nm dan nilai polidispersitas (PDI) sebesar 2,03. Penggunaan koproses kasein-kolagen sebagai eksipien menghasilkan sediaan serum dengan viskositas rendah.
ABSTRACT
The longan seed (Dimocarpus longan Lour.) contains polyphenol compounds which have antioxidant activity and tyrosinase inhibitory effect. Phytosomes are lipid nanovesicles which can be used as a drug carrier systems especially drugs from plant extracts that can increase the absorption of the drug. The aim of this study is to formulate a serum containing longan seed extract phytosome using a coprocess of casein-collagen as an excipient. Casein was used in combination with collagen because of its benefit in maintaining skin elasticity. The DPPH (2,2-diphenyl-1-pycril hydrazil) radical scavenging method was used to determine the value of efficient concentration (EC50) of longan seed extract, whereas tyrosinase inhibitory assay of longan seed extract was measured based on dopachrome measurement to obtain the value of inhibition concentaration (IC50). The entrapment efficiency of the phytosome was calculated based on determination of total phenolic compounds in the supernatant by using the Folin-Ciocalteu method. The EC50 values ​​of longan seed extract was 6.58 μg/mL, the Z-average values was 382.59 nm and the polidispersity index (PDI) was 2,03. Tyrosinase inhibitory assay showed the IC50 values was 1795.93 μg/mL. Phytosome formulation with phosphatidylcholine and extract ratio of 1.5:1 showed the entrapment efficiency of 65,88%. The use of casein-collagen coprocess as an excipient resulted in a serum with low viscosity.
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2014
S54909
UI - Skripsi Membership  Universitas Indonesia Library
cover
Ismail Fahmi
Analisis Praktik Residensi Keperawatan Medikal Bedah Pada Pasien Dengan Low Cardiac Output Syndrome Post Cabg Menggunakan The Dynamic Nurse-Patient Relationship Model Di Rumah Sakit Jantung Dan Pembuluh Darah Harapan Kita = Analysis of Surgical Nursing Medical Nursing Practices on Patients with Low Cardiac Output Syndrome after CABG Using The Dynamic Nurse-Patient Relationship Model in Jantung Dan Pembuluh Darah Harapan Kita Hospital
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Consensus Statement of Standards for Interventional Cardiovascular Nursing Practice menetapkan  domain standar praktik interventional keperawatan kardiovaskular  meliputi mampu berfikir kritis dan menganalisis intervensi kardiovaskular dalam praktik keperawatan, terlibat dalam hubungan terapeutik dan hubungan profesional untuk meningkatkan pelayanan dan pengalaman dalam pemberian asuhan keperawatan.  The dynamic nurse-patient relationship model telah digunakan sebagai teori dasar dalam memberikan asuhan keperawatan pada praktik keperawatan, yang menekankan  prinsip-prinsip dasar pemikiran kritis, pendekatan yang berpusat pada klien intervensi serta berorientasi pada tujuan, dan penggunaan  rekomendasi intervensi keperawatan berbasis bukti. Penerapan The dynamic nurse-patient relationship model pada praktik residensi menetapkan penurunan curah jantung sebagai diagnosis keperawatan utama pada pasien kelolaan utama dan 30 pasien lainnya, dengan cardiac care sebagai pilihan intervensi keperawatan untuk mengoptimalkan fungsi jantung dan menurunkan beban kerja jantung. CAM-ICU sebagai instrumen diagnostik memiliki keandalan yang sempurna untuk menilai delirium pasca pembedahan jantung (sensitifitas 100% dan spesitifitas 100%), lain halnya BHIS sebagai istrumen untuk menilai risiko kejadian SSI pasca pembedahan jantung memiliki keandalan yang sedang ( sensitifitas 70% dan spesitifitas 67%), artinya BHIS perlu dikembangkan kembali dengan memperhatikan faktor-faktor yang berhubungan dengan kejadian SSI.

 

The Consensus Statement of Standards for Interventional Cardiovascular Nursing Practice has established the standard domain of interventional cardiovascular nursing practices which includes the ability to think critically and to analyze cardiovascular interventions in nursing practice, engaging in therapeutic relationships and professional relationships to improve service and experience in providing nursing care. The dynamic nurse-patient relationship model has been used as a primary theory, providing nursing care approach into nursing practice which emphasizes the basic principles of critical thinking, client-centered and intervention-oriented approaches, and the use of evidence-based nursing intervention recommendations. The dynamic nurse-patient relationship model in residency practice establishes a decrease in cardiac output as the main nursing diagnosis in primary management patients and 30 other patients, with cardiac care as the choice of nursing intervention to optimize cardiac function and reduce cardiac workload. CAM-ICU as a diagnostic instrument has perfect reliability to assess delirium after cardiac surgery (100% sensitivity and 100% specificity). BHIS as an instrument to assess the risk of SSI events after cardiac surgery has moderate reliability (70% sensitivity and 67% specificity), meaning that BHIS needs to be developed by taking into account the factors related to SSI events.

 

Keywords: ida jean orlando, delirium, CAM-ICU, surgical site infection, cardiac surgery, low cardiac output, respiratory muscle training.

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Depok: Fakultas Ilmu Keperawatan Universitas Indonesia , 2020
TA-Pdf
UI - Tugas Akhir  Universitas Indonesia Library
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