[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.] |
S57906-Siti Julia.pdf :: Unduh