@misc{eprints27850,
           month = {Juli},
           title = {STUDY PENGARUH PENAMBAHAN POLIETILEN GLIKOL 6000 TERHADAP KESTABILAN ENZIM PROTEASE DARI
Rhizopus oligosporus},
          author = {1317011041 Maya Retna Sari},
         address = {Universitas Lampung},
       publisher = {Fakultas Matematika dan Ilmu Pengetahuan Alam},
            year = {2017},
             url = {http://digilib.unila.ac.id/27850/},
        abstract = {Penelitian ini bertujuan untuk meningkatkan kestabilan enzim protease yang diisolasi dari jamur Rhizopus oligosporus dengan penambahan polietilen glikol 6000. Penelitian ini dilakukan dengan beberapa tahapan, yaitu isolasi, pemurnian dan karakterisasi. Pada tahap pemurnian, enzim dimurnikan dengan cara fraksinasi dan dialisis. Hasil pemurnian menunjukkan bahwa enzim protease mempunyai aktivitas spesifik sebesar 931,149 U/mg yang kemurniannya meningkat 4 kali dibandingkan dengan ekstrak kasar. Selanjutnya, enzim ditmbahkan polietilen glikol 6000 konsentrasi 12, 14, dan 24\%, lalu dikarakterisasi. Enzim hasil pemurnian mempunyai pH 8; suhu optimum 35?C; KM = 90,9 mg/mL substrat; Vmaks = 50 ?mol/mL.menit; t? = 15 menit; ki = 0,044 menit-1; dan ?Gi = 101,885 KJ/mol. Enzim dengan penambahan polietilen glikol 6000 konsentrasi 12, 14, dan 24\% mempunyai pH 8; suhu optimum 45?C; berturut-turut mempunyai nilai KM = 83,3 mg/mL substrat, 33,3 mg/mL substrat, dan 25 mg/mL substrat; nila Vmaks = 33,3 ?mol/mL.menit, 20 ?mol/mL.menit, dan 14,28 ?mol/mL.menit; nilai t? = 20 menit, 26 menit, dan 31 menit; nilai ki = 0,034 menit-1, 0,026 menit-1, dan 0,022 menit-1; serta nilai ?Gi = 102,569 KJ/mol, 122,438 KJ/mol, dan 122,901 KJ/mol. Penurunan nilai ki serta peningkatan t? dan ?Gi menunjukkan bahwa enzim dengan penambahan polietilen glikol 6000 lebih stabil daripada enzim hasil pemurnian.


Kata kunci : Protease, Rhizopus oligosporus, polietilen glikol 6000.



ABSTRACT

This research was aimed to improve the stability protease enzyme isolated from Rhizopus oligosporus with addition polyethylene glycol 6000. Some sequential steps in this research were including isolation, purification, and characterization. At the purification step, the protease enzyme was purified by fractionation and dialysis. The result showed a specific activity of protease enzyme of 931.149 U/mg, increased of 4 folds than the crude extract. And then, enzyme added polyethylene glycol 6000 concentrations 12, 14, and 24\% then characterized. The purified enzyme has pH 8; optimum temperature at 35?C; KM = 90.9 mg/mL substrate; Vmax = 50 ?mol/mL.minute; t? = 15 minutes; ki = 0.044 minute-1; and ?Gi = 101.885 KJ/mol. Enzymes with addition of polyethylene glycol 6000 concentrations 12, 14, and 24\% had pH 8; optimum temperature at 45?C; consecutively had the values of KM = 83.3 mg/mL substrate, 33.3 mg/mL substrate, and 25 mg/mL substrate; the values of Vmax = 33.3 ?mol/mL.minute, 20 ?mol/mL.minute, and 14.28 ?mol/mL.minute; the  values of t? = 20 minutes, 26 minutes, and 31 minutes; the values of ki = 0.034 minute-1, 0.026 minute-1, and 0.022 minute-1; and the values of ?Gi = 102.569 KJ/mol, 122.438 KJ/mol, and 122.901 KJ/mol. Decreased of ki, increased of half-life (t?) and ?Gi indicated that the protease enzyme with addition polyethylene glycol 6000 more stable than the purified enzyme.


Key words : Protease, Rhizopus oligosporus, polyethylene glycol 6000.

}
}