Ezra Rheinsky Tiarsa, 1317011019 (2017) AMOBILISASI ENZIM α-AMILASE DARI Bacillus subtilis ITBCCB148 MENGGUNAKAN BENTONIT. FAKULTAS MATEMATIKA DAN ILMU PENGETAHUAN ALAM, UNIVERSITAS LAMPUNG.
|
File PDF
ABSTRAK (ABSTRACT).pdf Download (142Kb) | Preview |
|
![[img]](http://digilib.unila.ac.id/style/images/fileicons/text.png) |
File PDF
SKRIPSI FULL.pdf Restricted to Hanya pengguna terdaftar Download (3016Kb) |
|
|
File PDF
SKRIPSI TANPA BAB PEMBAHASAN.pdf Download (2769Kb) | Preview |
Abstrak (Berisi Bastraknya saja, Judul dan Nama Tidak Boleh di Masukan)
ABSTRACT In this study, the α-amylase from Bacillus subtilis ITBCCB148 was immobilized by using bentonite. The aims of this research were to increase the stability of α-amylase and to help in their economic reuse. The steps of this research were done as following: production, isolation, purification, immobilization, and characterization of purified and immobilized enzymes. The result showed that the purified enzyme from CMC cation column chromatography process has specific activity was 10387.11 U mg-1. It was higher 12 times than the crude extract. The optimum temperature of purified enzyme was 60oC, KM = 6.18 mg mL-1 substrate, and Vmax = 909.09 µmol mL-1 min-1. The optimum temperature of immobilized enzyme was 75oC, KM = 12.19 mg mL-1 substrate, and Vmax = 88.50 µmol mL-1 min-1. Residual activities of purified and immobilized enzyme in the study of thermal stability on 60oC for 100 minutes approximately were 12% and 43%. The activity of immobilized enzyme was maintained significantly even after 5 reuses. The kinetic studies of purified enzyme were obtained t½ = 42.00 minutes, ki = 0.0165 min-1, and ΔGi = 104.57 kJ mol-1. The kinetic studies of immobilized enzyme were obtained t½ = 88.85 minutes, ki = 0.0078 min-1, and ΔGi = 106.65 kJ mol-1. Based on the increase of half-time (t½), decrease of ki, and increase of ΔGi, the immobilization by using bentonite can improve the stability of α-amylase from B. subtilis ITBCCB148. Keywords: α-amylase, Bacillus subtilis ITBCCB148, immobilization, bentonite ABSTRAK Pada penelitian ini telah dilakukan amobilisasi enzim α-amilase dari Bacillus subtilis ITBCCB148 menggunakan matriks bentonit. Penelitian ini bertujuan untuk meningkatkan kestabilan enzim dan agar enzim dapat digunakan secara berulang. Tahap penelitian ini meliputi proses produksi, isolasi, pemurnian, amobilisasi, dan karakterisasi enzim murni dan amobil. Hasil penelitian menunjukkan bahwa aktivitas spesifik enzim α-amilase hasil pemurnian hingga tahap kromatografi penukar kation menggunakan CMC adalah 10387,11 U mg-1 dan kemurniannya meningkat 12 kali dibandingkan dengan ekstrak kasar enzim. Enzim α-amilase hasil pemurnian memiliki suhu optimum 60oC, KM = 6,18 mg mL-1 substrat, dan Vmaks = 909,09 µmol mL-1 menit-1. Enzim α-amilase hasil amobilisasi memiliki suhu optimum 75oC, KM = 12,19 mg mL-1 substrat, dan Vmaks = 88,50 µmol mL-1 menit-1. Aktivitas sisa enzim murni dan enzim amobil dalam uji stabilitas termal pada suhu 60oC selama 100 menit berturut-turut sebesar 12% dan 43%. Enzim amobil dapat digunakan berulang hingga 5 kali. Data kinetika enzim hasil pemurnian diperoleh t½ = 42,00 menit, ki = 0,0165 menit-1, dan ΔGi = 104,57 kJ mol-1. Data kinetika enzim hasil amobilisasi diperoleh t½ = 88,85 menit, ki = 0,0078 menit-1, dan ΔGi yaitu 106,65 kJ mol-1. Berdasarkan penurunan nilai ki, peningkatan nilai ΔGi dan waktu paruh (t½), diketahui bahwa amobilisasi menggunakan bentonit dapat meningkatkan stabilitas enzim α-amilase dari B. subtilis ITBCCB148. Kata kunci: α-amilase, Bacillus subtilis ITBCCB148, amobilisasi, bentonit
| Jenis Karya Akhir: | Skripsi |
|---|---|
| Subyek: | > Q Science (General) |
| Program Studi: | FAKULTAS MIPA > Prodi Kimia |
| Pengguna Deposit: | 59156688 . Digilib |
| Date Deposited: | 21 Jul 2017 06:22 |
| Terakhir diubah: | 21 Jul 2017 06:22 |
| URI: | http://digilib.unila.ac.id/id/eprint/27360 |
Actions (login required)
 |
Lihat Karya Akhir |
