Sigit Mariyanto, (1327011034) (2015) ISOLASI, PEMURNIAN, DAN MODIFIKASI KIMIA ENZIM α-AMILASE DARI Aspergillus niger L-51 MENGGUNAKAN SENYAWA ASAM GLIOKSILAT. Masters thesis, UNIVERSITAS LAMPUNG.
|
File PDF
ABSTRAK.pdf Download (25Kb) | Preview |
|
|
File PDF
COVER DALAM.pdf Download (24Kb) | Preview |
|
|
File PDF
COVER DEPAN.pdf Download (39Kb) | Preview |
|
|
File PDF
DAFTAR GAMBAR.pdf Download (16Kb) | Preview |
|
|
File PDF
DAFTAR ISI.pdf Download (22Kb) | Preview |
|
|
File PDF
DAFTAR LAMPIRAN.pdf Download (17Kb) | Preview |
|
|
File PDF
DAFTAR TABEL.pdf Download (14Kb) | Preview |
|
|
File PDF
MENYETUJUI.pdf Download (280Kb) | Preview |
|
|
File PDF
MENGESAHKAN.pdf Download (219Kb) | Preview |
|
|
File PDF
MOTO.pdf Download (24Kb) | Preview |
|
|
File PDF
PERSEMBAHAN.pdf Download (92Kb) | Preview |
|
|
File PDF
RIWAYAT HIDUP.pdf Download (12Kb) | Preview |
|
|
File PDF
SANWACANA.pdf Download (12Kb) | Preview |
|
|
File PDF
SURAT PERNYATAAN.pdf Download (306Kb) | Preview |
|
|
File PDF
BAB I.pdf Download (24Kb) | Preview |
|
|
File PDF
BAB II.pdf Download (176Kb) | Preview |
|
|
File PDF
BAB III.pdf Download (46Kb) | Preview |
|
![[img]](http://digilib.unila.ac.id/style/images/fileicons/text.png) |
File PDF
BAB IV.pdf Restricted to Hanya pengguna terdaftar Download (192Kb) |
|
|
File PDF
BAB V.pdf Download (12Kb) | Preview |
|
|
File PDF
DAFTAR PUSTAKA.pdf Download (31Kb) | Preview |
Abstrak (Berisi Bastraknya saja, Judul dan Nama Tidak Boleh di Masukan)
Penelitian ini bertujuan untuk meningkatkan kestabilan enzim α-amilase hasil pemurnian dengan modifikasi kimia. Untuk mencapai tujuan tersebut telah dilakukan isolasi, pemurnian, dan modifikasi kimia enzim hasil pemurnian, serta karakterisasi enzim hasil pemurnian dan hasil modifikasi. Isolasi enzim dilakukan dengan cara sentrifugasi dingin, sedangkan pemurnian enzim dilakukan dengan fraksinasi menggunakan amonium sulfat dan dialisis. Aktivitas enzim α-amilase ditentukan dengan menggunakan metode Fuwa dan Mandels, sedangkan kadar protein ditentukan dengan metode Lowry. Hasil penelitian menunjukkan bahwa aktivitas spesifik enzim α-amilase hasil pemurnian 11.235,104 U/mg, meningkat 8,7 kali dibandingkan dengan ekstrak kasar enzim yang mempunyai aktivitas spesifik 1.286,853 U/mg. Enzim hasil pemurnian ini mempunyai pH optimum 5,5; suhu optimum 45oC; KM = 2,738 mg/mL substrat; Vmaks = 238,095 μmol/mL.menit. Stabilitas thermal enzim hasil pemurnian ditunjukan dengan data – data sebagai berikut: ki = 0,0142 menit-1; t1/2 = 48,803 menit dan ΔGi = 100,134 kJ/mol. Enzim hasil modifikasi menggunakan asam glioksilat dengan derajat modifikasi 50, 63,3 dan 73,3 % mempunyai pH optimum 5,5; suhu optimum 45oC; KM berturut-turut sebagai berikut: 4,115; 3,466 dan 3,964 mg/mL; Vmaks berturut-turut sebagai berikut: 384,615; 333,333 dan 357,143 μmol/mL.menit. Stabilitas thermal enzim hasil modifikasi dengan derajat modifikasi 50; 63,3; dan 73,3 % ditunjukan dengan data – data sebagai berikut : ki berturut-turut sebagai berikut: 0,0126, 0,0109 dan 0,0102 menit-1; waktu paruh berturut-turut sebagai berikut: 55,000; 63,578 dan 67,941 menit; ΔGi berturut-turut sebagai berikut: 100,452; 100,835 dan 101,010 kJ/mol. Stabilitas termal enzim α-amilase hasil modifikasi meningkat sebesar 1,1-1,4 kali berdasarkan penurunan nilai ki, peningkatan waktu paruh, dan ΔGi. Kata kunci : Aspergillus niger L-51, α-amilase, modifikasi kimia, asam glioksilat. ABSTRAK BAHASA INGGRIS This research is aimed to improve the stability of chemical modified α-amylase. A series experiments including isolation, purification, chemical modification and characterization of the enzymes. The enzyme was harvested by cold centrifugation, while the purification was carried out by using ammonium sulfate fractionation and dialysis. The enzyme activity was determined using Fuwa and Mandels, while the protein content was determined by Lowry method. The results showed that the specific activity of the α-amylase purification was 11,235.104 U/mg, it has been increased 8.7 times compared with the crude extract that has a specific activity 1,286.853 U/mg. All purified enzyme has optimum pH and temperature is 5.5 and 45oC respectively. The KM of these enzyme = 2.738 mg/ mL substrate and the Vmax of these enzyme = 238.095 mol/mL.minutes. The thermal stability of the purified enzyme indicated values as follows: ki = 0.0142 min-1; t1/2 = 48.803 minutes and ΔGi = 100.134 kJ/mol. The enzyme was then modified by using glyoxylic acid with a degree of modification of 50, 63.3, and 73.3 %. All modified enzyme has optimum pH and temperature is 5.5 and 45oC respectively. The KM of these enzyme were : 4.115, 3.466, and 3.964 mg/ml respectively. The Vmax of these enzyme were : 384.615, 333.333, and 357.143 mol/ml.minutes respectively. The thermal stability of the enzyme modified with a degree of modification 50, 63.3, and 73.3%. The ki of these enzyme were : 0.0126, 0.0109, and 0.0102 min-1 respectively. The half-life of these enzyme were : 55.000, 63.578, and 67.941 minutes respectively. The ΔGi of these enzyme were : 100.452, 100.835, and 101.010 kJ/mol respectively. The thermal stability of the modified enzyme increased by 1.1 to 1.4 times based impairment ki, increased half-life, and ΔGi. Keywords: Aspergillus niger L-51, α-amylase, chemical modification, glyoxylic acid.
| Jenis Karya Akhir: | Tesis (Masters) |
|---|---|
| Subyek: | > QD Chemistry |
| Program Studi: | FAKULTAS MIPA > Prodi Magister Ilmu Kimia |
| Pengguna Deposit: | 6672775 . Digilib |
| Date Deposited: | 21 Jan 2016 03:00 |
| Terakhir diubah: | 21 Jan 2016 03:00 |
| URI: | http://digilib.unila.ac.id/id/eprint/18787 |
Actions (login required)
 |
Lihat Karya Akhir |
