RACHMADINI AULIA, - (2022) MODIFIKASI BOBOT MOLEKUL KARAGENAN HASIL EKSTRAKSI NaOH pH 9 MENGGUNAKAN VARIASI KONSENTRASI ENZIM ALFA AMILASE. Skripsi thesis, Sekolah Tinggi Farmasi Indonesia.
![[img]](http://repository.stfi.ac.id/style/images/fileicons/text.png) |
Text
S_PSSF_A181032_Title.pdf Download (1MB) |
|
Text
S_PSSF_A181032_Chapter1.pdf Restricted to Repository staff only Download (310kB) |
|
Text
S_PSSF_A181032_Chapter2.pdf Restricted to Repository staff only Download (366kB) |
|
Text
S_PSSF_A181032_Chapter3.pdf Restricted to Repository staff only Download (451kB) |
|
Text
S_PSSF_A181032_Chapter4.pdf Restricted to Repository staff only Download (535kB) |
|
Text
S_PSSF_A181032_Chapter5.pdf Restricted to Repository staff only Download (181kB) |
|
Text
S_PSSF_A181032_Appendix.pdf Restricted to Repository staff only Download (903kB) |
Abstract
Karagenan adalah senyawa polisakarida yang memiliki banyak fungsi terutama dalam bidang farmasi. Saat ini karagenan memiliki bobot molekul besar dan aplikasinya sebagai eksipien masih terbatas. Bobot molekul merupakan variabel penting pada karagenan karena berhubungan langsung dengan sifat fisika-kimia polimer. Salah satu cara untuk memperoleh bobot molekul lebih kecil dengan cara hidrolisis enzimatis. Tujuan dari penelitian ini untuk mengetahui profil penurunan bobot molekul karagenan dari variasi konsentrasi alfa amilase dalam proses modifikasi. Metode yang digunakan dengan inkubasi larutan karagenan 1% dengan variasi konsentrasi enzim alfa amilase 0,25%, 0,5% dan 1% pada suhu 38oC selama 120 menit dalam keadaan pH 5,6 dan diamati setiap 30 menit. Perhitungan bobot molekul karagenan dengan menghitung viskositas intrinsik larutan yang kemudian dihubungkan dengan persamaan Mark-Houwink, diketahui bahwa viskositas intrinsik berbanding lurus dengan bobot molekul. Hasil akhir menunjukan bahwa variasi kosentrasi enzim dapat menurunkan bobot molekul karagenan di setiap interval waktu inkubasi pada semua variasi konsentrasi enzim, dan tidak terdapat signifikansi antara variasi konsentrasi enzim alfa amilase 0,25%, 0,5%, dan 1% terhadap penurunan bobot molekul karagenan hasil ekstraksi NaOH pH 9. --- Carrageenan is a polysaccharide compound that has many functions, especially in the pharmaceutical field. At present, carrageenan has a large molecular weight and its application as an excipient is still limited. Molecular weight is an important variable in carrageenan as it is directly related to the physico-chemical properties of the polymer. One way to get a smaller molecular weight is enzymatic hydrolysis. The purpose of this study was to determine the profile of carrageenan molecular weight reduction by variations in the concentration of alpha-amylase in the modification process. The method used was incubation of a 1% carrageenan solution with fluctuations in the concentration of the alpha-amylase enzyme of 0.25%, 0.5% and 1% at 38°C for 120 minutes at a pH of 5.6 and one observation every 30 minutes. Calculation of Carrageenan Molecular Weight by calculating the intrinsic viscosity of the solution, which is then connected to the MarkHouwink equation, it is known that intrinsic viscosity is directly proportional to molecular weight. The final results showed that the variation in enzyme concentration could reduce the molecular weight of carrageenan in each incubation time interval for all variations in enzyme concentration, but there was no significant difference between variations the concentration of alpha-amylase enzyme 0.25%, 0.5 % and 1% on molecular weight decrease of carrageenan extracted from NaOH pH 9.
| Item Type: | Thesis (Skripsi) |
|---|---|
| Uncontrolled Keywords: | Karagenan, Bobot Molekul, hidrolisis enzimatik, alfa amilase, Viskositas intrinsik. --- Carrageenan, Molecular Weight, enzymatic hydrolysis, alphaamylase, Iintrinsic viscosity. |
| Subjects: | Q Science > Q Science (General) |
| Divisions: | Program Studi S1 Farmasi |
| Depositing User: | pustakawan - - |
| Date Deposited: | 14 Sep 2024 13:44 |
| Last Modified: | 14 Sep 2024 13:44 |
| URI: | http://repository.stfi.ac.id/id/eprint/1210 |
Actions (login required)
 |
View Item |
