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题名: Immobilization of Alcaligenes faecalis Penicillin G Acylase on Epoxy-Type Supports
作者: Sun, J.1;  Zhou, Y.2;  Yuan, Z.3;  Xu, G.1
通讯作者: 许国旺
刊名: APPLIED BIOCHEMISTRY AND MICROBIOLOGY
发表日期: 2009-09-01
DOI: 10.1134/S0003683809050032
卷: 45, 期:5, 页:478-483
收录类别: SCI
文章类型: Article
部门归属: 18
项目归属: 1808
产权排名: 1;1
WOS标题词: Science & Technology ;  Life Sciences & Biomedicine
类目[WOS]: Biotechnology & Applied Microbiology ;  Microbiology
研究领域[WOS]: Biotechnology & Applied Microbiology ;  Microbiology
英文摘要: Alcaligenes faecalis penicillin G acylase has several desired features over other penicillin G acylases and its use in industry requires immobilization. In this work, two novel supports ZH-EP (epoxy type) and ZH-HA (epoxy-amino type) were used to immobilize Alcaligenes faecalis penicillin G acylase (AfPGA) with Eupergit C as reference. The saturation of immobilized protein on ZH-EP (269 mg/g, 116 h) and ZH-HA (296 mg/g, 15 h) was obtained more rapidly than Eupergit C (197 mg/g, 260 h). And the activity of immobilized AfPGA on ZH-EP (520 U/g) and ZH-HA (2200 U/g) was higher than that on Eupergit C (310 U/g). The propertics of three immobilized enzymes were compared and no obvious difference was observed, which indicated that ZH-EP and ZH-HA were promised in industry.
关键词[WOS]: MULTIPOINT COVALENT ATTACHMENT ;  SALT-INDUCED IMMOBILIZATION ;  ACTIVATED SUPPORTS ;  GLUTARYL ACYLASE ;  PROTEINS ;  PERFORMANCE ;  SEPABEADS ;  ENZYMES ;  TOOL
语种: 英语
原文出处: 查看原文
WOS记录号: WOS:000269885800003
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/102167
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
2.E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China
3.Chinese Acad Sci, Shanghai Inst Life Sci, Inst Biochem & Cell Biol, Shanghai 200031, Peoples R China

Recommended Citation:
Sun, J.,Zhou, Y.,Yuan, Z.,et al. Immobilization of Alcaligenes faecalis Penicillin G Acylase on Epoxy-Type Supports[J]. APPLIED BIOCHEMISTRY AND MICROBIOLOGY,2009,45(5):478-483.
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