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Hybrid Magnetic Cross-Linked Enzyme Aggregates of Phenylalanine Ammonia Lyase from Rhodotorula glutinis
Alternative TitlePLoS One
Cui, Jian dong1,2,3; Cui, Li li1,2; Zhang, Song ping2,4; Zhang, Yu fei2; Su, Zhi guo2; Ma, Guang hui2
2014-05-13
Source PublicationPLOS ONE
ISSN1932-6203
Volume9Issue:5Pages:8
AbstractNovel 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 K-m of enzyme in CLEAs and HM-PAL-CLEAs, V-max 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.; 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 K-m of enzyme in CLEAs and HM-PAL-CLEAs, V-max 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.
KeywordBovine Serum-albumin Penicillin-g Acylase Organic Media Silica Cleas Immobilization Biocatalysts Stabilization Coaggregation Nanoparticles
SubtypeArticle
WOS HeadingsScience & Technology
DOI10.1371/journal.pone.0097221
URL查看原文
Indexed BySCI
Language英语
WOS KeywordBOVINE SERUM-ALBUMIN ; PENICILLIN-G ACYLASE ; ORGANIC MEDIA ; SILICA ; CLEAS ; IMMOBILIZATION ; BIOCATALYSTS ; STABILIZATION ; COAGGREGATION ; NANOPARTICLES
WOS Research AreaScience & Technology - Other Topics
WOS SubjectMultidisciplinary Sciences
WOS IDWOS:000336369200072
Citation statistics
Cited Times:30[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/10892
Collection研究所(批量导入)
Affiliation1.Hebei Univ Sci & Technol, Coll Biosci & Bioengn, Res Ctr Fermentat Engn Hebei, Shijiazhuang, Peoples R China
2.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing, Peoples R China
3.Tianjin Univ Sci & Technol, Key Lab Ind Microbiol, Tai Da Dev Area, Minist Educ, Tianjin, Peoples R China
4.Collaborat Innovat Ctr Chem Sci & Engn Tianjin, Tianjin, Peoples R China
Recommended Citation
GB/T 7714
Cui, Jian dong,Cui, Li li,Zhang, Song ping,et al. Hybrid Magnetic Cross-Linked Enzyme Aggregates of Phenylalanine Ammonia Lyase from Rhodotorula glutinis[J]. PLOS ONE,2014,9(5):8.
APA Cui, Jian dong,Cui, Li li,Zhang, Song ping,Zhang, Yu fei,Su, Zhi guo,&Ma, Guang hui.(2014).Hybrid Magnetic Cross-Linked Enzyme Aggregates of Phenylalanine Ammonia Lyase from Rhodotorula glutinis.PLOS ONE,9(5),8.
MLA Cui, Jian dong,et al."Hybrid Magnetic Cross-Linked Enzyme Aggregates of Phenylalanine Ammonia Lyase from Rhodotorula glutinis".PLOS ONE 9.5(2014):8.
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