Immobilization of Penicillin G Acylase on Oxirane-Modified Mesoporous Silicas-Reference-Cited by-同舟云学术

Immobilization of Penicillin G Acylase on Oxirane-Modified Mesoporous Silicas

Published:2009-01-07 Issue:3 Volume:25 Page:1807-1812
ISSN:0743-7463
Container-title:Langmuir
language:en
Short-container-title:Langmuir

Author:

Sun Hong¹,Bao Xiao Ying¹,Zhao X. S.¹

Affiliation:

1. Institute of Multifunctional Materials (IMM), Laboratory of New Fiber Materials and Modern Textile, College of Chemistry, Chemical Engineering and Environment, Qingdao University, Qingdao 266071, China, and Department of Chemical and Biomolecular Engineering, National University of Singapore, 4 Engineering Drive 4, Singapore 117576

Publisher

American Chemical Society (ACS)

Subject

Electrochemistry,Spectroscopy,Surfaces and Interfaces,Condensed Matter Physics,General Materials Science

Link

https://pubs.acs.org/doi/pdf/10.1021/la803480c

Reference41 articles.

1. Penicillin acylase has a single-amino-acid catalytic centre

2. Crystal structures of penicillin acylase enzyme-substrate complexes: structural insights into the catalytic mechanism 1 1Edited by K. Nagai

3. Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft

4. Immobilization of Penicillin G Acylase: The Key to Optimum Performance

5. Multifunctional Epoxy Supports: A New Tool To Improve the Covalent Immobilization of Proteins. The Promotion of Physical Adsorptions of Proteins on the Supports before Their Covalent Linkage

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