PENGARUH PENAMBAHAN GLISEROL TERHADAP KESTABILAN ENZIM α-AMILASE DARI Aspergillus fumigatus
| Main Author: | Nurul Nadila, 1617011078 |
|---|---|
| Format: | Bachelors NonPeerReviewed Book Report |
| Terbitan: |
FAKULTAS MATEMATIKA DAN ILMU PENGETAHUAN ALAM
, 2020
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| Subjects: | |
| Online Access: |
http://digilib.unila.ac.id/65457/1/ABSTRAK.pdf http://digilib.unila.ac.id/65457/2/SKRIPSI%20FULL.pdf http://digilib.unila.ac.id/65457/3/SKRIPSI%20TANPA%20BAB%20PEMBAHASAN.pdf http://digilib.unila.ac.id/65457/ |
Daftar Isi:
- Enzim α-amilase adalah enzim yang mengkatalisis hidrolisis dari ikatan α-1,4 glikosidik polisakarida untuk menghasilkan monomer-monomernya. Enzim yang digunakan dalam industri harus stabil pada suhu dan pH tinggi. Penelitian ini bertujuan meningkatkan kestabilan enzim α-amilase dari Aspergillus fumigatus hasil pemurnian dengan penambahan gliserol. Pemurnian enzim dilakukan dengan fraksinasi menggunakan ammonium sulfat dan diaslisis. Aktivitas enzim ditentukan menggunakan metode Fuwa dan Mandels, serta kadar protein ditentukan menggunakan metode Lowry. Hasil penelitian menunjukkan enzim hasil pemurnian memiliki aktivitas spesifik sebesar 1,377 U/mg dan meningkat sebanyak 8,1 kali dibandingkan dengan ekstrak kasar enzim yang memiliki aktivitas spesifik sebesar 0,170 U/mg. Enzim hasil pemurnian memiliki pH optimum 5,5 ; suhu optimum 55°C, KM = 2,45 mg mL-1, Vmaks = 19,23 μmol mL-1 menit-1, ki = 0,0052 menit-1, t1/2 = 133,26 menit, dan ∆Gi = 106,109 kJ/mol. Enzim setelah penambahan gliserol 0,5 ; 1 dan 1,5 M memiliki pH optimum 5,5 ; suhu optimum 55°C. Stabilitas termal gliserol 0,5 M ki = 0,0044 menit-1, t1/2 = 157,5 menit, ∆Gi = 106,564 kJ/mol; gliserol 1 M ki = 0,0038 menit-1, t1/2 = 182,36 menit, ∆Gi = 106,964 kJ/mol dan gliserol 1,5 M ki = 0,0031 menit-1, t1/2 = 223,54 menit, ∆Gi = 107,520 kJ/mol. Penambahan gliserol pada enzim α-amilase dapat meningkatkan kestabilan enzim sebanyak 1,2-1,7 kali dibandingkan dengan enzim hasil pemurnian ditunjukkan dengan dengan penurunan nilai ki, peningkatan t1/2 dan ∆Gi. Kata kunci : α-amilase, Aspergillus fumigatus, penambahan zat aditif, gliserol ABSTRACT The α-amylase is an enzyme that catalyzes the hydrolysis of α-1,4 glycosidic bond polysaccharides to produce a monomers. Enzymes used in industry must be stable at high temperatures and pH. The objective of research is to increase the stability of the α-amylase by Aspergillus fumigatus from the purified with the addition of glycerol. The enzyme purification was carried out by fractionation using ammonium sulfate and diaclysis. Enzyme activity was determined using the Fuwa and Mandels method, and protein content was determined using the Lowry method. The results of the purified enzyme had a specific activity was 1.377 U/mg and increased 8.1 times compared to the crude extract of the enzyme which had a specific activity was 0.170 U/mg. The purified enzyme has an optimum pH of 5.5, optimum temperature of 55°C, KM = 2.45 mg mL-1, Vmaks = 19.23 μmol mL-1 menit-1, ki = 0.0052 menit-1, t1/2 = 133.26 minutes, and ∆Gi = 106.109 kJ/mol. Enzymes with the addition of glycerol 0.5 ; 1 and 1.5 M have an optimum pH of 5.5, optimum temperature of 55°C. Thermal stability of glycerol 0.5 M ki = 0.0044 menit-1, t1/2 = 157.5 minutes, ∆Gi = 106.564 kJ/mol; glycerol 1 M ki = 0.0038 menit-1, t1/2 = 182.36 minutes, ∆Gi = 106,964 kJ/mol; and glycerol 1.5 M ki = 0.0031 menit-1, t1/2 = 223.54 minutes, ∆Gi = 107.520 kJ/mol. The addition of glycerol to the α-amylase enzyme can increase the stability of the enzyme 1.2-1.7 times compared to the purified enzyme which indicated by decreasing the value of ki, increasing t1/2 and ∆Gi. Keywords : α-amylase, Aspergillus fumigatus, addition of additives, glycerol