Desi Meriyanti, 1017011057 (2014) PENINGKATAN KESTABILAN ENZIM SELULASE DARI JAMUR Aspergillus niger L-51 DENGAN AMOBILISASI MENGGUNAKAN BENTONIT. FAKULTAS MATEMATIKA DAN ILMU PENGETAHUAN ALAM, UNIVERSITAS LAMPUNG.
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Abstrak (Berisi Bastraknya saja, Judul dan Nama Tidak Boleh di Masukan)
Abstrak Indonesia Pada penelitian ini telah dilakukan amobilisasi enzim selulase dari Aspergillus niger L-51 menggunakan bentonit untuk meningkatkan stabilitas enzim tersebut. Adapun tahapan yang dilakukan dalam penelitian ini meliputi : produksi, isolasi, pemurnian, amobilisasi menggunakan bentonit dan karakterisasi enzim selulase hasil pemurnian sebelum dan setelah amobilisasi meliputi penentuan suhu optimum, nilai KM dan Vmaks, pengulangan enzim amobil serta uji stabilitas termal enzim. Hasil penelitian menunjukkan bahwa aktivitas spesifik enzim selulase hasil pemurnian 20,9993 U/mg, meningkat 8,6 kali dibandingkan dengan ekstrak kasar enzim selulase yang mempunyai aktivitas spesifik 2,4401 U/mg. Enzim selulase hasil pemurnian mempunyai suhu optimum 60oC; KM = 38,368 mg/mL substrat; Vmaks = 3,075 μmol/mL.menit; ki = 0,037 menit-1; waktu paruh (t1/2) = 18 menit dan ΔGi = 103,914 kJ/mol. Enzim selulase hasil amobilisasi menggunakan bentonit mempunyai suhu optimum 65oC; KM = 12,764 mg/mL substrat; Vmaks = 0,834 μmol/mL.menit; ki = 0,036 menit-1; waktu paruh (t1/2) = 19 menit dan ΔGi = 103,991 kJ/mol Berdasarkan penurunan nilai ki, peningkatan waktu paruh (t1/2) dan nilai ΔGi, diketahui bahwa amobilisasi menggunakan bentonit dapat meningkatkan stabilitas enzim selulase dari Aspergillus niger L-51. Abstract The aim of this research is to increase the stability of cellulase from Aspergillus nigerL-51 using immobilization method by bentonite. Several procedures were performed to achieve the aim, which were production, isolation, purification, immobilization using bentonite and characterization of the purified enzyme before and after immobilization which include determinations of optimum temperature, KM and Vmax.values, the repeat use of immobilized enzyme and thermal stability. The results showed that the specific activity of the purified cellulase was 20.9993 U/mg, increased of 8.6 times compared to that of the crude extract which has 2.4401 U/mg. The characters of purified cellulase were optimum temperature 60˚C; KM = 38.368 mg/mL substrate; Vmax. = 3.075 µmol/mL.min; ki = 0.037 min-1; half-life (t1/2) = 18 minutesand ∆Gi= 103.914 kJ/mol. Thecharacters of the immobilized cellulase were optimum temperature 65˚C; KM = 12.764 mg/mL substrate; Vmax. = 0.834 µmol/mL.min.;ki = 0.036 min-1; half-life (t1/2) = 19 minutes and ∆Gi = 103.991 kJ/mol, respectively. Based on the decrease ofki value, increase of t1/2 and ∆Gi, it is proven that the immobilization method could be used to increase the stability of cellulase.
| Jenis Karya Akhir: | Skripsi |
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| Subyek: | |
| Program Studi: | FAKULTAS MIPA > Prodi Kimia |
| Pengguna Deposit: | 007538 . Digilib |
| Date Deposited: | 29 Sep 2014 07:17 |
| Terakhir diubah: | 29 Sep 2014 07:17 |
| URI: | http://digilib.unila.ac.id/id/eprint/3579 |
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