Enzyme-catalyzed polymerizations of ε-caprolactone: Effects of initiator on product structure, propagation kinetics, and mechanism

Macromolecules

Volumn 29, Issue 24, 1996, Pages 7759-7766

  Henderson, Lori A ^a   Svirkin, Yuri Y ^a   Gross, Richard A ^a   Kaplan, David L ^b   Swift, Graham ^c  

^a University of Massachusetts Lowell   (United States)

^b Biotechnology Division   (United States)

^c ROHM AND HAAS COMPANY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLIC ACIDS; CATALYSIS; CATALYST ACTIVITY; COMPOSITION EFFECTS; ENZYME KINETICS; INITIATORS (CHEMICAL); MOLECULAR STRUCTURE; MOLECULAR WEIGHT; SYNTHESIS (CHEMICAL);

BUTANOL; BUTYLAMINES; CHAIN TRANSFER; COPROLACTONES; PORCINE PANCREATIC LIPASE (PPL);

RING OPENING POLYMERIZATION;

EID: 0030285310     PISSN: 00249297     EISSN: None     Source Type: Journal    
DOI: 10.1021/ma960821h     Document Type: Article

References (17)

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11. 1H NMR spectrum no. 38167M, 1984.
12. n did not vary significantly with the addition of water. Thus, it is concluded that, under the incubation conditions used in this work, hydrolysis in the absence of enzyme is negligible.
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15. The rate dependence on the concentration of the catalyst was also observed in experiments where the concentration of PPL was decreased from 750 to 375 mg for ε-CL polymerization initiated with water (0.12 mmol). The results for percent monomer conversion decreased from 100 to 86% after a 96 h reaction time (unpublished results).
16. See citation 16 in ref 3.
17. Bisht, K; Svirkin, Y.; Gross, R.; Kaplan, D.; Swift, G., manuscript in preparation.