Journal article
Enzymatic synthesis of a sucrose‐containing linear polyester in nearly anhydrous organic media
Biotechnology and bioengineering, Vol.37(7), pp.639-646
03/25/1991
DOI: 10.1002/bit.260370706
PMID: 18600655
Abstract
A variety of enzymes have been found to acylate sucrose in anhydrous pyridine. The enzymic reaction is highly selective; with trifluoroethylbutyrate as ester donor, enzyme‐catalyzed transesterification of sucrose yielded sucrose 1′‐butyrate and sucrose 6, 1′‐dibutyrate. No sucrose–tributyrates were formed. Using a similar technique, a long‐chain linear sucrose polyester has been prepared using Proleather, an alkaline protease from a Bacillus sp. This protease catalyzes the esterification of sucrose with bis(2, 2, 2‐trifluoroethyladipate) in a 1:1 ratio to yield a sucrose‐containing polyester with Mw = 2100 and Mn = 1600 for a polydispersity of 1. 31. Polymers with molecular weights in excess of 13, 000 have been prepared by this enzymic approach, indicating that molecules containing over 30 sucrose units have been produced. The polyester is extremely water soluble and soluble in polar organic solvents. As with the sucrose dibutyrate, the polyester has ester linkages at the C6 and C1′ positions on the sucrose. The polyester can be depolymerized using Proleather in aqueous buffer, pH7. After 9 days in aqueous buffer, Proleather catalyzed the breakdown of the polyester to an Mw of ca. 900. This sucrose‐containing polyester may have applications as a water‐absorbent, biodegradable plastic for use as diapers and hygienic products, water‐treatment chemicals, and components of drug delivery systems.
Details
- Title: Subtitle
- Enzymatic synthesis of a sucrose‐containing linear polyester in nearly anhydrous organic media
- Creators
- Damodar R PatilDavid G RethwischJonathan S Dordick
- Resource Type
- Journal article
- Publication Details
- Biotechnology and bioengineering, Vol.37(7), pp.639-646
- Publisher
- Wiley Subscription Services, Inc., A Wiley Company; Hoboken
- DOI
- 10.1002/bit.260370706
- PMID
- 18600655
- ISSN
- 0006-3592
- eISSN
- 1097-0290
- Number of pages
- 8
- Language
- English
- Date published
- 03/25/1991
- Academic Unit
- Chemical and Biochemical Engineering
- Record Identifier
- 9984003466802771
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