Imobilisasi Lipase pada Kitosan Serbuk dengan Metode Pengikatan Silang dan Uji Aktivitas Transesterifikasinya

Wikan Mahargyani, Tri Joko Raharjo, Winarto Haryadi

Abstract


Telah dilakukan imobilisasi lipase pada kitosan serbuk dengan metode pengikatan silang. Penelitian ini bertujuan untuk mengetahui kondisi optimum proses imobilisasi dan aktivitas katalitik lipase terimobilisasi. Enzim lipase diimobilisasikan pada kitosan serbuk menggunakan glutaraldehid sebagai senyawa penaut silang. Parameter yang dipelajari untuk menentukan kondisi optimum imobilisasi meliputi pH pelarutan enzim, nilai derajat deasetilasi, perbandingan mol kitosan dengan glutaraldehid, dan konsentrasi enzim. Enzim lipase terimobilisasi dan enzim lipase bebas diuji aktivitas, stabilitas termal, dan kemampuan penggunaan ulangnya melalui reaksi transesterifikasi minyak kelapa sawit menggunakan metanol. Hasil penelitian menunjukkan bahwa kondisi optimum imobilisasi diperoleh saat enzim dilarutkan pada buffer fosfat pH 6, perbandingan mol kitosan dengan glutaraldehid 4:1, dan konsentrasi enzim 5%. Enzim lipase terimobilisasi mempunyai stabilitas termal yang lebih rendah tetapi mempunyai kemampuan penggunaan ulang yang lebih baik daripada enzim lipase bebas.

 


Keywords


lipase; kitosan; imobilisasi; pengikatan silang; transesterifikasi

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References


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DOI: http://dx.doi.org/10.30870/educhemia.v2i2.1454

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