LILY NUR SAFITRI, lilinur403@gmail.com (2022) PENINGKATAN KESTABILAN ENZIM. FAKULTAS MATEMATIKA DAN ILMU PENGETAHUAN ALAM, UNIVERSITAS LAMPUNG. (Submitted)
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Abstrak (Berisi Bastraknya saja, Judul dan Nama Tidak Boleh di Masukan)
ABSTRAK PENINGKATAN KESTABILAN ENZIM α-AMILASE DARI Aspergillus fumigatus DENGAN PENAMBAHAN GLUTARALDEHID Oleh Lily Nur Safitri Pada penelitian ini, telah dilakukan penambahan glutaraldehid pada enzim α-amilase yang diisolasi dari A. fumigatus. Ekstrak kasar enzim dimurnikan dengan fraksinasi menggunakan amonium sulfat, dan dialisis. Aktivitas enzim ditentukan dengan metode Fuwa, dan metode Mandels. Kadar protein ditentukan dengan metode Lowry. Hasil penelitian menunjukkan aktivitas spesifik α-amilase hasil pemurnian sebesar 520,51 U/mg, meningkat 8,93 kali dibandingkan dengan ekstrak kasar yang mempunyai aktivitas spesifik sebesar 58,31 U/mg. Enzim hasil pemurnian mempunyai pH optimum 5; suhu optimum 55°C; KM = 10,80 mg/mL substrat dan Vmaks = 10,13 μmol/mL-1 menit-1. Uji stabilitas termal enzim hasil pemurnian pada suhu 60°C selama 100 menit memiliki aktivitas sisa 12,00% dengan nilai ki = 0,0228 menit-1; t1/2 = 30,39 menit dan ΔGi = 103,639 kJ/mol-1. Enzim hasil penambahan glutaraldehid dengan konsentrasi 0,02; 0,04; dan 0,06% mempunyai pH optimum 6,5; suhu optimum 55°C; KM berturut-turut sebesar = 12,85; 21,73; dan 14,54 mg/mL substrat dan nilai Vmaks = 7,37; 9,85; dan 7,37 μmol/mL-1 menit-1, nilai ki = 0,0082; 0,0083; dan 0,0084 menit-1; t1/2 = 84,51; 83,49; dan 82,50 menit dan ΔGi = 106,491; 106,463; dan 106,436 kJ/mol-1. Terjadi peningkatan waktu paruh (t1/2) dan ΔGi serta penurunan nilai ki enzim hasil penambahan glutaraldehid dibandingkan dengan enzim hasil pemurnian sebesar 2,7 sampai 2,8 kali. Kata kunci: α-amilase, stabilitas enzim, A. fumigatus, glutaraldehid. In this research, the addition of glutaraldehyde to the α-amylase enzyme isolated from A. fumigatus has been carried out. Enzyme crude extract was purified by fractionation using ammonium sulfate, and dialysis. Enzyme activity was determined by Fuwa method, and Mandels method. Protein content was determined by Lowry method. The results showed that the specific activity of α-amylase purified was 520.51 U/mg, an increase of 8.93 times from the crude extract which had a specific activity of 58.31 U/mg. The purified enzyme has an optimum pH of 5; optimum temperature 55°C; KM = 10.80 mg/mL substrate and Vmax = 10.13 mol/mL-1 min-1. Thermal stability test of purified enzyme at 60°C for 100 minutes had a residual activity of 12.00% with a value of ki = 0.0228 min-1; t1/2 = 30.39 min and ΔGi = 103.639 kJ/mol-1. Enzyme resulted from the addition of glutaraldehyde with a concentration of 0.02%; 0.04%; and 0.06% have an optimum pH of 6.5; optimum temperature 55°C; KM = 12.85; 21.73; and 14.54 mg/mL of substrate consecutively and the value of Vmax = 7.37; 9.85; and 7.37 mol/mL-1, ki value = 0.0082; 0.0083; and 0.0084 min-1; t1/2 = 84.51; 83.49; and 82.50 minutes and ΔGi = 106.491; 106.463; and 106.436 kJ/mol-1. There was an increase in half-life (t1/2) and ΔGi as well as a decrease in the ki value of the enzyme resulting from the addition of glutaraldehyde compared to the enzyme by 2.7 to 2.8 times. Keywords: α-amylase, enzyme stability, A. fumigatus, glutaraldehyde.
Jenis Karya Akhir: | Skripsi |
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Subyek: | 000 Ilmu komputer, informasi dan pekerjaan umum 000 Ilmu komputer, informasi dan pekerjaan umum > 001 Ilmu pengetahuan |
Program Studi: | FAKULTAS MIPA > Prodi Kimia |
Pengguna Deposit: | 2301021817 . Digilib |
Date Deposited: | 23 Dec 2022 04:28 |
Terakhir diubah: | 23 Dec 2022 04:28 |
URI: | http://digilib.unila.ac.id/id/eprint/68039 |
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