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BukuShort Communication: Purification of methanol dehydrogenase from mouth methylotrophic bacteria of tropical region (article of Malaysian Journal of Microbiology Vol.7 No.4 December 2011)
Bibliografi
Author: Waturangi, Diana Elizabeth ; Marko, Nico ; Suhartono, Maggy Thenawidjaja
Topik: methanol dehydrogenase; methylotrophs; enzyme purification; JABFUNG-DEW-2015-03
Bahasa: (EN )    
Penerbit: Malaysian Society for Microbiology     Tempat Terbit: Penang, Malaysia    Tahun Terbit: 2011    
Jenis: Article - diterbitkan di jurnal ilmiah internasional
Fulltext: MJM v7 n4 p226.pdf (118.43KB; 2 download)
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Abstract
Aims: Purification of methanol dehydrogenase (MDH) from methylotrophic bacteria was conducted to obtain pure enzyme for further research and industrial applications due to the enzyme’s unique activity that catalyzes oxidation of methanol as an important carbon source in methylotrophic bacteria.
Methodology and Results: The enzyme was screened from methylotrophic bacteria isolated from human mouth. Purification of this enzyme was conducted using ammonium sulphate precipitation followed by cation exchange chromatography. Two types of media were used to produce the enzymes: luria broth and standard mineral salts media (MSM). MSM produced MDH with higher specific activity than LB. Specific activity was also increased along with the purification steps. Application of ammonium sulphate increased the purity of enzyme and was more effective for the enzyme produced in LB. Using sepharose increased the enzyme activity 10 -57 folds.
Conclusion, significant and impact of this study: With this, ammonium sulphate precipitation coupled with single cation exchange chromatographic system has been proved to provide sufficient purified of methanol dehydrogenase from methylotrophic bacteria origin of human mouth with high specific activity for further application.
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