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All Journal Media Penelitian dan Pengembangan Kesehatan Biota: Jurnal Ilmiah Ilmu-Ilmu Hayati
Naiola, Elidar
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Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Decision Sciences, Operations Research & Management Public Health

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KEMAMPUAN BACILLUS LICHENIFORMIS DALAM MEMPRODUKSI ENZIM PROTEASE YANG BERSIFAT ALKALIN DAN TERMOFILIK Soeka, Yati Sudaryati; Rahayu, Sri Hartin; Setianingrum, Ninu; Naiola, Elidar
Media Penelitian dan Pengembangan Kesehatan Vol 21, No 2 Jun (2011)
Publisher : Badan Penelitian dan Pengembangan Kesehatan

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22435/mpk.v21i2 Jun.109.

Abstract

The aim of the research was to measure the production of protease enzyme in alkaline and thermophilic of bacteria Bacillus licheniformis. The protease enzyme signed by clear zone arround the bacteria colonies on medium which contain 1% skimmed milk. The activities of protease enzyme treated  by the period of incubation, temperature and pH, which measured by spectrophotometer at ? 280 nm. The results showed that the highest production of protease activity at 2 days incubation was 150,52 U/mL. At temperature 50°C and pH 10 they were 123,34  U/mL and 193,14 U/mL.
Karakterisasi Enzim Komersial Siklodekstrin Glukanotransferase Naiola, Elidar; Widhyastuti, Nunuk
Biota : Jurnal Ilmiah Ilmu-Ilmu Hayati Vol 13, No 2 (2008): June 2008
Publisher : Universitas Atma Jaya Yogyakarta

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (115.944 KB) | DOI: 10.24002/biota.v13i2.2676

Abstract

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 tempetature and pH for enzyme reaction were 450C to 550C and pH 5.0 to 8.0, respectively. The CGTase was relatively stable after heating at 550C 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 Cu2+ was the strongest inhibitor, with presence of 1mM Cu2+ the residual activity of CGTase was 24.4%. Results 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).
Co-Authors NUNUK WIDHYASTUTI Rahayu, Sri Hartin Setianingrum, Ninu Yati Sudaryati Soeka