AMOBILISASI ENZIM SELULASE DARI Aspergillus niger L-51 MENGGUNAKAN ZEOLIT

SINTA DEWI O, 1317011067 (2017) AMOBILISASI ENZIM SELULASE DARI Aspergillus niger L-51 MENGGUNAKAN ZEOLIT. FAKULTAS MATEMATIKA DAN ILMU PENGETAHUAN ALAM , UNIVERSITAS LAMPUNG.

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Abstrak

proses sakarifikasi bahan berselulosa, deterjen, industri makanan, dan pengolahan limbah pabrik kertas. Penggunaan enzim dalam proses industri harus memenuhi syarat-syarat tertentu yaitu enzim harus stabil pada suhu tinggi dan tahan terhadap keadaan pH ekstrim. Sedangkan, pada umumnya enzim hanya mampu bekerja pada kondisi fisiologis dan tidak tahan terhadap kondisi ekstrim. Penelitian ini bertujuan untuk memproduksi dan mengisolasi enzim selulase dari jamur Aspergillus niger L- 51 yang kemudian dimurnikan dengan tahap fraksinasi dan dialisis, lalu ditingkatkan stabilitasnya melalui amobilisasi menggunakan zeolit. Aktivitas spesifik enzim selulase hasil pemurnian meningkat 7 kali lipat dibandingkan dengan ekstrak kasar enzim. Ekstrak kasar enzim memiliki aktivitas spesifik sebesar 5,3944 U/mg dan enzim hasil pemurnian memiliki aktivitas spesifik sebesar 38,0292 U/mg. Suhu optimum enzim hasil pemurnian pada suhu 50oC sedangkan suhu optimum enzim hasil amobilisasi pada suhu 75oC. Aktivitas sisa yang dihasilkan pada uji stabilitas termal pada suhu 50oC selama 100 menit terhadap enzim hasil pemurnian adalah sebesar 5% sedangkan terhadap enzim hasil amobilisasi sebesar 23%. Data kinetika enzim hasil pemurnian yaitu Vmaks = 4,7400 μmol/mL/menit, KM = 1,9400 mg/mL, ki = 0,024 menit-1, t1/2 = 28,87 menit-1 dan ΔGi = 100,345 kJ/mol. Sedangkan untuk enzim hasil amobilisasi memiliki data kinetika enzim yaitu Vmaks = 1,4000 μmol/mL/menit, KM = 0,9900 mg/mL, ki = 0,013 menit-1, t1/2 = 53,30 menit-1, dan ΔGi = 102,175 kJ/mol. Berdasarkan hasil penelitian ini, disimpulkan bahwa enzim hasil amobilisasi menggunakan zeolit mengalami peningkatan waktu paruh sebesar 1,84 kali dibandingkan enzim hasil pemurnian. Kata Kunci : selulase, Aspergillus niger L-51, Amobilisasi, zeolit. ABSTRACT Cellulase is a complex enzyme that cuts gradually the cellulose chain into glucose. In many biotechnology applications, cellulase is used in the process of saccharification of cellulosic materials, detergents, food industry, and paper waste mill processing. The use of enzymes in industrial processes must satisfy certain conditions i.e enzymes must be stable at high temperatures and resistant in extreme pH conditions. Whereas, in general enzyme is only able to work on physiological conditions and not resistant to extreme conditions. The purpose of this study was to produce and isolate the cellulase enzyme from Aspergillus niger L-51 fungi which is then purified by fractionation and dialysis stage, then enhanced its stability through immobilization using zeolite. The specific activity of the purified cellulase enzyme increased 7 times higer than the crude extract enzyme. The crude extract enzyme has a specific activity of 5.3944 U/mg and the purified enzyme has a specific activity of 38.0292 U/mg. The optimum temperature of the purified enzyme was 50oC while the optimum temperature of the immobilized enzyme was at 75°C. The residual activity resulted in thermal stability test at temperature 50oC for 100 min against purification enzyme was 5% while the immobilization enzyme of was 23%. The kinetics data of the purified enzyme were Vmax = 4.7400 μmol/ mL/ min, KM = 1.9400 mg / mL, ki = 0,024 min-1, t1/2 = 28.87 min-1 and ΔGi = 100.345 kJ/mol, while the immobilization enzyme were Vmax = 1.4000 μmol/mL/min, KM = 0.9900 mg/mL, ki = 0.013 min-1, t1/2 = 53.30 min-1, and ΔGi = 102.175 kJ/mol. Based on the results of this study, it was concluded that the amobilization enzyme of using zeolite had an increase in halflife of 1.84 times compared to the purification enzyme. Key Word : Cellulase, Aspergillus niger L-51, Immobilization, zeolite.

Tipe Karya Ilmiah: Skripsi
Subyek: Q Science (General) > QD Chemistry
Program Studi: Fakultas MIPA > Prodi Kimia
Depositing User: 59819379 . Digilib
Date Deposited: 23 Jan 2018 02:39
Last Modified: 23 Jan 2018 02:39
URI: http://digilib.unila.ac.id/id/eprint/29860

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