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Borate buffer dramatically enhances the activity of poly(ethylene glycol)-α-chymotrypsin complex catalytically active in anhydrous isooctane than conventional phosphate buffer even at low concentration

Borate buffer dramatically enhances the activity of poly(ethylene glycol)-α-chymotrypsin complex... Poly(ethylene glycol) 4000-α-chymotrypsin (with a molar ratio of the polymer/enzyme of 8:1) complex prepared from borate buffer solutions had ca. 6000- and 26-fold higher activity than native α-chymotrypsin and a complex prepared using a conventional phosphate buffer, respectively, even at lower concentration (0.0474 mol g−1 enzyme) than that of inorganic salts which were required for the enzyme activation. These results suggested that relatively hydrophobic buffers are desirable for preparing modified enzymes that are catalytically active in organic media and contributed to develop more effective methodology for the optimal design of enzyme preparations for nonaqueous enzymology. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biotechnology Letters Springer Journals

Borate buffer dramatically enhances the activity of poly(ethylene glycol)-α-chymotrypsin complex catalytically active in anhydrous isooctane than conventional phosphate buffer even at low concentration

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References (25)

Publisher
Springer Journals
Copyright
Copyright © 2001 by Kluwer Academic Publishers
Subject
Life Sciences; Biotechnology; Organic Chemistry; Biochemistry, general; Microbiology; Animal Anatomy / Morphology / Histology
ISSN
0141-5492
eISSN
1573-6776
DOI
10.1023/A:1010345318275
Publisher site
See Article on Publisher Site

Abstract

Poly(ethylene glycol) 4000-α-chymotrypsin (with a molar ratio of the polymer/enzyme of 8:1) complex prepared from borate buffer solutions had ca. 6000- and 26-fold higher activity than native α-chymotrypsin and a complex prepared using a conventional phosphate buffer, respectively, even at lower concentration (0.0474 mol g−1 enzyme) than that of inorganic salts which were required for the enzyme activation. These results suggested that relatively hydrophobic buffers are desirable for preparing modified enzymes that are catalytically active in organic media and contributed to develop more effective methodology for the optimal design of enzyme preparations for nonaqueous enzymology.

Journal

Biotechnology LettersSpringer Journals

Published: Oct 23, 2004

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