Karakterisasi Enzim Komersial Siklodekstrin Glukanotransferase  

Oleh:

Naiola, Elidar ; Widhyastuti, Nunuk

Jenis: Article from Journal - ilmiah nasional - tidak terakreditasi DIKTI
Dalam koleksi: Biota Jurnal Ilmiah Ilmu-ilmu Hayati vol. 13 no. 2 (Jul. 2008), page 89-96.
Topik: cyclodextrin glucanotransferase; bacillus macerans; purification; characterization

Ketersediaan

Perpustakaan Pusat (Semanggi) Nomor Panggil: BB74 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada

Lihat Detail Induk

Isi artikel

The objective of this study is to investigate the characteristic of commercial enzyme Cyclodextrin Glucanotrasferase (CGTase) from Bacillus macerans. The CGTase was purified by dialysis, gel fitration and ion exchange chromatography. Study on Characterization of the enzyme showed that the hydrolytic activity of CGTase was 480 U/mg, the optimum temperature and pH for enzyme reaction were 45 C to 55 C for 10 minutes, and maintained its activity at the pH 5.0 to 9.0. The enzyme activity was inhibited by the presence of 1 mM metal ions and cause CGTase lost approximately 40% of its activity. Among the metal ions it was found that Cu 2+ was the strongest inhibitor, with presence of 1mM Cu2+ the residual activity of CGTase was 24.4%. Result of purification showed that specific activities of the enzyme during purification were 269 U/mg (crude enzyme); 955 U/mg (dialysis); 481 U/mg (gel fitrations); and 544 U/mg (ion exchange chromatography).

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