Biocatalysis in Polymer Science by Richard A. Gross and H. N. Cheng (Eds.)

By Richard A. Gross and H. N. Cheng (Eds.)

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1992, 6, 523. ; Kobayashi, S. Macromolecules 1998, 31, 554. ; Marechal, Ε. J Polym. ,Part A, Polym. Chem. 1997, 35, 3331. ; Marechal, Ε. A. ACS Polym. Prepr. 2000, 41(1), 213. A. Biomacromolecules, 2000, 1(3), 501. ; Gross, R. A. ACS Polym. Prepr. 2000, 41(2),1828. ; Gross, R. A. ACS Polym. Prepr. 2000, 41(2), 1935. 64. ; Gross, R. A. ACS Symp. Ser. (this volume). 65. For example, (a) Glycochemistry; Wang, P. ; Bertozzi, C. R. ; M. Dekker, New York, 2001. (b) Preparative Carbohydrate Chemistry; Hanessian, S.

Lett. 2000, 7, 800-801 21. J. Biotechnol. Bioengin. 1997, 55, 227-239. 22. , Biochemistry, 1992, 31, 2588-2598 23. Akkara, J. ; Senecal, K. ; Kaplan D. L. J. Polym. , Part A: Polym. Chem. 1991, 29, 1561-1574. ch002 49 24. ; Herman, M. ; Dordick, J. S. Anal. Chim. Acta. 1998, 370, 251-258. 25. S. Biotech. Prog. 2000, 16, 513-516. 26. Alva, K. ; Marx, Κ. ; Tripathy, S. ; Akkara, J. ; Kaplan, D. L. Proc. SPIE-Int. Soc. Opt. Eng. 1997, 3040(Smart Materials Technologies), 200-210. 27. Patel, M. ; Sutaria, D.

Antarctica lipase catalyzed polymerizations showed M in the range of 330 to as high as 6,640, corresponding to a degree of polymerization (DP) of 17. 8 for the larger polymers. Complete conversion of monomer was obtained for C. antarctica lipase in acetonitrile, and therefore used in subsequent studies for the construction of the next library. ch002 n w Figure 1. Library 1: Synthesized using catalysts from different sources [C. antarctica lipase (CALB), Porcine pancreatic lipase (PPL), and Protex-6L (PRO)] and by varying reaction mediums (acetonitrile, acetone, and tert-amyl alcohol).

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