Publication

Atomistic Model for the Polyamide Formation from beta-Lactam Catalyzed by Candida antarctica Lipase B

Baum, I., Elsaesser, B., Schwab, L. W., Loos, K., Fels, G. & Elsässer, B., Apr-2011, In : ACS Catalysis. 1, 4, p. 323-336 14 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Baum, I., Elsaesser, B., Schwab, L. W., Loos, K., Fels, G., & Elsässer, B. (2011). Atomistic Model for the Polyamide Formation from beta-Lactam Catalyzed by Candida antarctica Lipase B. ACS Catalysis, 1(4), 323-336. https://doi.org/10.1021/cs1000398

Author

Baum, Iris ; Elsaesser, Brigitta ; Schwab, Leendert W. ; Loos, Katja ; Fels, Gregor ; Elsässer, Brigitta. / Atomistic Model for the Polyamide Formation from beta-Lactam Catalyzed by Candida antarctica Lipase B. In: ACS Catalysis. 2011 ; Vol. 1, No. 4. pp. 323-336.

Harvard

Baum, I, Elsaesser, B, Schwab, LW, Loos, K, Fels, G & Elsässer, B 2011, 'Atomistic Model for the Polyamide Formation from beta-Lactam Catalyzed by Candida antarctica Lipase B', ACS Catalysis, vol. 1, no. 4, pp. 323-336. https://doi.org/10.1021/cs1000398

Standard

Atomistic Model for the Polyamide Formation from beta-Lactam Catalyzed by Candida antarctica Lipase B. / Baum, Iris; Elsaesser, Brigitta; Schwab, Leendert W.; Loos, Katja; Fels, Gregor; Elsässer, Brigitta.

In: ACS Catalysis, Vol. 1, No. 4, 04.2011, p. 323-336.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Baum I, Elsaesser B, Schwab LW, Loos K, Fels G, Elsässer B. Atomistic Model for the Polyamide Formation from beta-Lactam Catalyzed by Candida antarctica Lipase B. ACS Catalysis. 2011 Apr;1(4):323-336. https://doi.org/10.1021/cs1000398


BibTeX

@article{5eac70a51e8e40fca3fedb8c4337abfb,
title = "Atomistic Model for the Polyamide Formation from beta-Lactam Catalyzed by Candida antarctica Lipase B",
abstract = "Candida antarctica lipase B (CALB) is an established biocatalyst for a variety of transesterification, amidation, and polymerization. reactions. In contrast to polyesters, poly amides are not yet generally accessible via enzymatic polymerization. In this regard, an enzyme-catalyzed ring-opening polymerization of beta-lactam (2-azetidinone) using CALB is the first example of an enzymatic polyamide formation yielding unbranched poly(beta-alanine), nylon 3. The performance of this polymerization, however, is poor, considering the maximum chain length of 18 monomer units with an average length of 8, and the molecular basis of the reaction so far is not understood. We have employed molecular modeling techniques using docking tools, molecular dynamics, and QM/MM procedures to gain insight into the mechanistic details of the various reaction steps involved. As a result, we propose a catalytic cycle for the oligomerization of beta-lactam that rationalizes the activation of the monomer, the chain elongation by additional beta-lactam molecules, and the termination of the polymer chain. In addition, the processes, leading to a premature chain termination are studied. Particularly, the QM/MM calculation enables an atomistic description of all eight steps involved in the catalytic cycle, which features an in situ-generated beta-alanine as the elongating monomer and which is compatible with the experimental findings.",
keywords = "Candida antarctica lipase B, enzyme catalysis, beta-lactam ring-opening, molecular modeling, enzymatic polymerization, enzyme acylation, RING-OPENING POLYMERIZATION, PROTEIN-LIGAND COMPLEXES, EPSILON-CAPROLACTONE, POLYESTERS, LACTONES, PREDICTION, RESOLUTION, MECHANISM, KINETICS, SOLVENT",
author = "Iris Baum and Brigitta Elsaesser and Schwab, {Leendert W.} and Katja Loos and Gregor Fels and Brigitta Els{\"a}sser",
year = "2011",
month = "4",
doi = "10.1021/cs1000398",
language = "English",
volume = "1",
pages = "323--336",
journal = "ACS Catalysis",
issn = "2155-5435",
publisher = "AMER CHEMICAL SOC",
number = "4",

}

RIS

TY - JOUR

T1 - Atomistic Model for the Polyamide Formation from beta-Lactam Catalyzed by Candida antarctica Lipase B

AU - Baum, Iris

AU - Elsaesser, Brigitta

AU - Schwab, Leendert W.

AU - Loos, Katja

AU - Fels, Gregor

AU - Elsässer, Brigitta

PY - 2011/4

Y1 - 2011/4

N2 - Candida antarctica lipase B (CALB) is an established biocatalyst for a variety of transesterification, amidation, and polymerization. reactions. In contrast to polyesters, poly amides are not yet generally accessible via enzymatic polymerization. In this regard, an enzyme-catalyzed ring-opening polymerization of beta-lactam (2-azetidinone) using CALB is the first example of an enzymatic polyamide formation yielding unbranched poly(beta-alanine), nylon 3. The performance of this polymerization, however, is poor, considering the maximum chain length of 18 monomer units with an average length of 8, and the molecular basis of the reaction so far is not understood. We have employed molecular modeling techniques using docking tools, molecular dynamics, and QM/MM procedures to gain insight into the mechanistic details of the various reaction steps involved. As a result, we propose a catalytic cycle for the oligomerization of beta-lactam that rationalizes the activation of the monomer, the chain elongation by additional beta-lactam molecules, and the termination of the polymer chain. In addition, the processes, leading to a premature chain termination are studied. Particularly, the QM/MM calculation enables an atomistic description of all eight steps involved in the catalytic cycle, which features an in situ-generated beta-alanine as the elongating monomer and which is compatible with the experimental findings.

AB - Candida antarctica lipase B (CALB) is an established biocatalyst for a variety of transesterification, amidation, and polymerization. reactions. In contrast to polyesters, poly amides are not yet generally accessible via enzymatic polymerization. In this regard, an enzyme-catalyzed ring-opening polymerization of beta-lactam (2-azetidinone) using CALB is the first example of an enzymatic polyamide formation yielding unbranched poly(beta-alanine), nylon 3. The performance of this polymerization, however, is poor, considering the maximum chain length of 18 monomer units with an average length of 8, and the molecular basis of the reaction so far is not understood. We have employed molecular modeling techniques using docking tools, molecular dynamics, and QM/MM procedures to gain insight into the mechanistic details of the various reaction steps involved. As a result, we propose a catalytic cycle for the oligomerization of beta-lactam that rationalizes the activation of the monomer, the chain elongation by additional beta-lactam molecules, and the termination of the polymer chain. In addition, the processes, leading to a premature chain termination are studied. Particularly, the QM/MM calculation enables an atomistic description of all eight steps involved in the catalytic cycle, which features an in situ-generated beta-alanine as the elongating monomer and which is compatible with the experimental findings.

KW - Candida antarctica lipase B

KW - enzyme catalysis

KW - beta-lactam ring-opening

KW - molecular modeling

KW - enzymatic polymerization

KW - enzyme acylation

KW - RING-OPENING POLYMERIZATION

KW - PROTEIN-LIGAND COMPLEXES

KW - EPSILON-CAPROLACTONE

KW - POLYESTERS

KW - LACTONES

KW - PREDICTION

KW - RESOLUTION

KW - MECHANISM

KW - KINETICS

KW - SOLVENT

U2 - 10.1021/cs1000398

DO - 10.1021/cs1000398

M3 - Article

VL - 1

SP - 323

EP - 336

JO - ACS Catalysis

JF - ACS Catalysis

SN - 2155-5435

IS - 4

ER -

ID: 5313680