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Enzyme‐catalyzed synthesis of sugar‐containing monomers and linear polymers
Author(s) -
Park OhJin,
Kim DaeYun,
Dordick Jonathan S.
Publication year - 2000
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/1097-0290(20001020)70:2<208::aid-bit10>3.0.co;2-0
Subject(s) - candida antarctica , adipate , chemistry , organic chemistry , polyester , lipase , monomer , condensation polymer , trehalose , yield (engineering) , catalysis , polymer , polymer chemistry , enzyme , materials science , metallurgy
Commercially available proteases and lipases were screened for their ability to acylate regioselectively sucrose and trehalose with divinyladipic acid ester. Opticlean M375 (subtilisin from Bacillus licheniformis ) was observed to form sucrose 1′‐O‐adipate and trehalose 6‐O‐adipate in anhydrous pyridine. Novozym‐435 (lipase B from Candida antarctica ) catalyzed the synthesis of sucrose 6, 6′‐O‐divinyladipate and trehalose 6, 6′‐O‐divinyladipate in acetone. These diesters were then employed as monomers in polycondensation reactions with various diols (aliphatic and aromatic) catalyzed by Novozym‐435 in organic solvents to yield linear polyesters with M w 's up to 22,000 Da. Spectroscopic analysis confirmed that only the vinyl end groups of sugar esters reacted in the enzymatic polymerization with the diol, and not the internal sugar‐adipate linkages. The two‐step enzymatic strategy to yield sugar‐based polyesters, which is the first report of its kind, results in higher molecular weights and faster reaction times than one‐step enzymatic polyester synthesis. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 70: 208–216, 2000.