TY  - GEN
CY  - UNIVERSITAS LAMPUNG
ID  - eprints27360
UR  - http://digilib.unila.ac.id/27360/
A1  - Ezra Rheinsky Tiarsa, 1317011019
Y1  - 2017/07/10/
N2  - ABSTRACT

In this study, the ?-amylase from Bacillus subtilis ITBCCB148 was immobilized by using bentonite.  The aims of this research were to increase the stability of      ?-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 ?Gi = 104.57 kJ mol-1.  The kinetic studies of immobilized enzyme were obtained t½ = 88.85 minutes, ki = 0.0078 min-1, and ?Gi = 106.65 kJ mol-1.  Based on the increase of half-time (t½), decrease of ki, and increase of ?Gi, the immobilization by using bentonite can improve the stability of ?-amylase from B. subtilis ITBCCB148.


Keywords: ?-amylase, Bacillus subtilis ITBCCB148, immobilization, bentonite


ABSTRAK

Pada penelitian ini telah dilakukan amobilisasi enzim ?-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 ?-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 ?-amilase hasil pemurnian memiliki suhu optimum 60oC, KM = 6,18 mg mL-1 substrat, dan Vmaks = 909,09 µmol mL-1 menit-1.  Enzim ?-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 ?Gi = 104,57 kJ mol-1.  Data kinetika enzim hasil amobilisasi diperoleh t½ = 88,85 menit, ki = 0,0078 menit-1, dan ?Gi yaitu 106,65 kJ mol-1.  Berdasarkan penurunan nilai ki, peningkatan nilai ?Gi dan waktu paruh (t½), diketahui bahwa amobilisasi menggunakan bentonit dapat meningkatkan stabilitas enzim ?-amilase dari B. subtilis ITBCCB148.


Kata kunci: ?-amilase, Bacillus subtilis ITBCCB148, amobilisasi, bentonit

PB  - FAKULTAS MATEMATIKA DAN ILMU PENGETAHUAN ALAM
TI  - AMOBILISASI ENZIM ?-AMILASE DARI Bacillus subtilis ITBCCB148 
MENGGUNAKAN BENTONIT 

AV  - restricted
ER  -