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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Cui, Jian-Dong Zhang, Si Sun, Li-Mei |
| Description | Author Affiliation: Cui JD ( Research Center for Fermentation Engineering of Hebei, College of Bioscience and Bioengineering, Hebei University of Science and Technology, Shijiazhang, People's Republic of China. cjd007cn@163.com) |
| Abstract | Cross-linked enzyme aggregates of phenylalanine ammonia lyase (PAL-CLEAs) from Rhodotorula glutinis were prepared. The effects of the type of aggregating agent, its concentration, and that of cross-linking agent were studied. PAL-CLEAs production was most effective using ammonium sulfate (40 % saturation), followed by cross-linking for 1 h with 0.2 % (v/v) glutaraldehyde. Moreover, the storage and operational stability of the resulting PAL-CLEAs were also investigated. Compared to the free enzyme, the PAL-CLEAs exhibited the expected increased stability of the enzyme against various deactivating conditions such as pH, temperature, denaturants, and organic solvents and showed higher storage stability than its soluble counterpart. Additionally, the reusability of PAL-CLEAs with respect to the biotransformation of L-phenylalanine was evaluated. PAL-CLEAs could be recycled at least for 12 consecutive batch reactions without dramatic activity loss, which should dramatically increase the commercial potential of PAL for synthesis of L: -phenylalanine. To the best of our knowledge, this is the first report of immobilization of PAL as cross-linked enzyme aggregates. |
| File Format | HTM / HTML |
| ISSN | 02732289 |
| Issue Number | 4 |
| Volume Number | 167 |
| e-ISSN | 15590291 |
| Journal | Applied Biochemistry and Biotechnology |
| Language | English |
| Publisher | Springer |
| Publisher Date | 2012-06-01 |
| Publisher Place | United States |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Discipline Biotechnology Biocatalysis Cross-linking Reagents Pharmacology Phenylalanine Ammonia-lyase Chemistry Metabolism Phenylalanine Biosynthesis Enzyme Stability Drug Effects Enzymes, Immobilized Hydrogen-ion Concentration Hydrophobic And Hydrophilic Interactions Organic Chemicals Protein Denaturation Rhodotorula Enzymology Solvents Temperature Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology |
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