Tags

Type your tag names separated by a space and hit enter

Polymerization of propyl malolactonate in the presence of Candida rugosa lipase.
Biomacromolecules 2003 Jan-Feb; 4(1):19-27B

Abstract

To gain better insight into mechanistic features of enzyme-catalyzed malolactonate polymerization, reactions with propyl malolactonate were analyzed while varying enzyme concentration, reaction media composition, and reaction temperature. Monomer conversion and product molecular weights were characterized by (1)H NMR and MALDI-TOF MS, respectively. A high extent of thermal polymerization of propyl malolactonate was observed, while the polymer chain length in all reactions was controlled by the elimination of alpha-hydrogen from propyl malolactonate with formation of a new initiator and the new chains. The most efficient enzymatic catalysis occurred in toluene (2.11 M monomer) at 60 degrees C. Candida rugosa lipase (10 wt %) accelerated polymerization 25-fold over the rate of thermal polymerization. The maximum poly(propyl malate) number-average molecular weight obtained was 5000 Da at 20 wt % enzyme with a polydispersity of 1.15. These values compare with 1800 Da and 1.5, respectively, in the absence of enzyme.

Authors+Show Affiliations

Department of Chemical and Biological Engineering, Department of Chemistry, and Bioengineering Center, Tufts University, 4 Colby Street, Medford, Massachusetts 02155, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

12523841

Citation

Panova, Anna A., et al. "Polymerization of Propyl Malolactonate in the Presence of Candida Rugosa Lipase." Biomacromolecules, vol. 4, no. 1, 2003, pp. 19-27.
Panova AA, Taktak S, Randriamahefa S, et al. Polymerization of propyl malolactonate in the presence of Candida rugosa lipase. Biomacromolecules. 2003;4(1):19-27.
Panova, A. A., Taktak, S., Randriamahefa, S., Cammas-Marion, S., Guerin, P., & Kaplan, D. L. (2003). Polymerization of propyl malolactonate in the presence of Candida rugosa lipase. Biomacromolecules, 4(1), pp. 19-27.
Panova AA, et al. Polymerization of Propyl Malolactonate in the Presence of Candida Rugosa Lipase. Biomacromolecules. 2003;4(1):19-27. PubMed PMID: 12523841.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Polymerization of propyl malolactonate in the presence of Candida rugosa lipase. AU - Panova,Anna A, AU - Taktak,Sonia, AU - Randriamahefa,Solo, AU - Cammas-Marion,Sandrine, AU - Guerin,Philippe, AU - Kaplan,David L, PY - 2003/1/14/pubmed PY - 2003/8/27/medline PY - 2003/1/14/entrez SP - 19 EP - 27 JF - Biomacromolecules JO - Biomacromolecules VL - 4 IS - 1 N2 - To gain better insight into mechanistic features of enzyme-catalyzed malolactonate polymerization, reactions with propyl malolactonate were analyzed while varying enzyme concentration, reaction media composition, and reaction temperature. Monomer conversion and product molecular weights were characterized by (1)H NMR and MALDI-TOF MS, respectively. A high extent of thermal polymerization of propyl malolactonate was observed, while the polymer chain length in all reactions was controlled by the elimination of alpha-hydrogen from propyl malolactonate with formation of a new initiator and the new chains. The most efficient enzymatic catalysis occurred in toluene (2.11 M monomer) at 60 degrees C. Candida rugosa lipase (10 wt %) accelerated polymerization 25-fold over the rate of thermal polymerization. The maximum poly(propyl malate) number-average molecular weight obtained was 5000 Da at 20 wt % enzyme with a polydispersity of 1.15. These values compare with 1800 Da and 1.5, respectively, in the absence of enzyme. SN - 1525-7797 UR - https://www.unboundmedicine.com/medline/citation/12523841/Polymerization_of_propyl_malolactonate_in_the_presence_of_Candida_rugosa_lipase_ L2 - https://dx.doi.org/10.1021/bm0255746 DB - PRIME DP - Unbound Medicine ER -