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DOI: 10.1371/journal.pone.0097221
论文题名:
Hybrid Magnetic Cross-Linked Enzyme Aggregates of Phenylalanine Ammonia Lyase from Rhodotorula glutinis
作者: Jian dong Cui; Li li Cui; Song ping Zhang; Yu fei Zhang; Zhi guo Su; Guang hui Ma
刊名: PLOS ONE
ISSN: 1932-6203
出版年: 2014
发表日期: 2014-5-13
卷: 9, 期:5
语种: 英语
英文关键词: Nanoparticles ; Magnetite ; Enzymes ; Enzyme immobilization ; Thermal stability ; Cross-linking ; Centrifugation ; Confocal laser microscopy
英文摘要: Novel hybrid magnetic cross-linked enzyme aggregates of phenylalanine ammonia lyase (HM-PAL-CLEAs) were developed by co-aggregation of enzyme aggregates with magnetite nanoparticles and subsequent crosslinking with glutaraldehyde. The HM-PAL-CLEAs can be easily separated from the reaction mixture by using an external magnetic field. Analysis by scanning electron microscopy (SEM) and confocal laser scanning microscopy (CLSM) indicated that PAL-CLEAs were inlayed in nanoparticle aggregates. The HM-PAL-CLEAs revealed a broader limit in optimal pH compared to free enzyme and PAL-CLEAs. Although there is no big difference in Km of enzyme in CLEAs and HM-PAL-CLEAs, Vmax of HM-PAL-CLEAs is about 1.75 times higher than that of CLEAs. Compared with free enzyme and PAL-CLEAs, the HM-PAL-CLEAs also exhibited the highest thermal stability, denaturant stability and storage stability. The HM-PAL-CLEAs retained 30% initial activity even after 11 cycles of reuse, whereas PAL-CLEAs retained 35% of its initial activity only after 7 cycles. These results indicated that hybrid magnetic CLEAs technology might be used as a feasible and efficient solution for improving properties of immobilized enzyme in industrial application.
URL: http://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0097221&type=printable
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/19873
Appears in Collections:过去全球变化的重建
影响、适应和脆弱性
科学计划与规划
气候变化与战略
全球变化的国际研究计划
气候减缓与适应
气候变化事实与影响

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作者单位: Research Center for Fermentation Engineering of Hebei, College of Bioscience and Bioengineering, Hebei University of Science and Technology, Shijiazhang, P R China;National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, HaiDian district, Beijing, P R China;Key Laboratory of Industry Microbiology, Ministry of Education, Tianjin University of Science and Technology, Tai Da Development Area, Tianjin, P R China;Research Center for Fermentation Engineering of Hebei, College of Bioscience and Bioengineering, Hebei University of Science and Technology, Shijiazhang, P R China;National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, HaiDian district, Beijing, P R China;National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, HaiDian district, Beijing, P R China;Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Tianjin, China;National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, HaiDian district, Beijing, P R China;National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, HaiDian district, Beijing, P R China;National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, HaiDian district, Beijing, P R China

Recommended Citation:
Jian dong Cui,Li li Cui,Song ping Zhang,et al. Hybrid Magnetic Cross-Linked Enzyme Aggregates of Phenylalanine Ammonia Lyase from Rhodotorula glutinis[J]. PLOS ONE,2014-01-01,9(5)
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