Retention Mechanism of β-Blockers on an Immobilized Cellulase. Relative Importance of the Hydrophobic And Ionic Contributions To Their Enantioselective and Nonselective Interactions-Reference-Cited by-同舟云学术

Retention Mechanism of β-Blockers on an Immobilized Cellulase. Relative Importance of the Hydrophobic And Ionic Contributions To Their Enantioselective and Nonselective Interactions

Published:2000-07-11 Issue:16 Volume:72 Page:3908-3915
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Götmar Gustaf¹,Fornstedt Torgny¹,Guiochon Georges¹

Affiliation:

1. Department of Pharmacy, BMC Box 580, S-751 23 Uppsala, Sweden, Department of Chemistry, The University of Tennessee, Knoxville, Tennessee 37996-1600, and Division of Chemical and Analytical Science, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831

Publisher

American Chemical Society (ACS)

Subject

Analytical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ac9914824

Reference25 articles.

1. Separation of enantiomers using cellulase (CBH I) silica as a chiral stationary phase

2. Cellulases as chiral selectors

3. The Three-Dimensional Crystal Structure of the Catalytic Core of Cellobiohydrolase I from Trichoderma reesei

4. Activity Studies and Crystal Structures of Catalytically Deficient Mutants of Cellobiohydrolase I fromTrichoderma reesei

5. High-resolution crystal structures reveal how a cellulose chain is bound in the 50 Å long tunnel of cellobiohydrolase I from Trichoderma reesei 1 1Edited by K. Nagai

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