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Sonochemically modified ovalbumin enhances enantioenrichment of some amino acids.
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- Additional Information
- Source:
Publisher: Elsevier Science Country of Publication: Netherlands NLM ID: 9433356 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-2828 (Electronic) Linking ISSN: 13504177 NLM ISO Abbreviation: Ultrason Sonochem Subsets: MEDLINE
- Publication Information:
Publication: Amsterdam : Elsevier Science
Original Publication: Oxford : Butterworth Heinemann, c1994-
- Subject Terms:
- Abstract:
As part of our efforts to develop a new method for chiral resolution of amino acids with sonochemically modified proteins, we present result that indicates how ovalbumin microspheres (OAMS) interact specifically with l-amino acids from a racemate in solution, leaving an excess of d-enantiomer in the permeate solution. Among different amino acids that interacted with the OAMS, tryptophan (Trp) was the most successfully resolved with 65% enantiomeric excess. A control experiment with native ovalbumin in solution did not show any chiral resolution of amino acids. Interestingly, when the OAMS were pretreated with racemic lysine (Lys) solution and then used for resolution of tryptophan the enantiomeric enrichment of d-tryptophan was raised to 98%. This unanticipated positive effect is discussed in terms of the structural correlation between Trp and Lys, which is less apparent in other amino acids such as phenylalanine.
(Copyright © 2019 Elsevier B.V. All rights reserved.)
- Contributed Indexing:
Keywords: Microspheres and Chiral separation; Ovalbumin; Sonication
- Accession Number:
0 (Amino Acids)
9006-59-1 (Ovalbumin)
- Publication Date:
Date Created: 20190828 Date Completed: 20191206 Latest Revision: 20191217
- Publication Date:
20231215
- Accession Number:
10.1016/j.ultsonch.2019.05.020
- Accession Number:
31450354
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